Full text data of MAPRE1
MAPRE1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Microtubule-associated protein RP/EB family member 1 (APC-binding protein EB1; End-binding protein 1; EB1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Microtubule-associated protein RP/EB family member 1 (APC-binding protein EB1; End-binding protein 1; EB1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15691
ID MARE1_HUMAN Reviewed; 268 AA.
AC Q15691; B2R6I7; E1P5M8; Q3KQS8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Microtubule-associated protein RP/EB family member 1;
DE AltName: Full=APC-binding protein EB1;
DE AltName: Full=End-binding protein 1;
DE Short=EB1;
GN Name=MAPRE1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH APC.
RX PubMed=7606712;
RA Su L.-K., Burrell M., Hill D.E., Gyuris J., Brent R., Wiltshire R.,
RA Trent J., Vogelstein B., Kinzler K.W.;
RT "APC binds to the novel protein EB1.";
RL Cancer Res. 55:2972-2977(1995).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-17, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V., Potts A., Barblan J., Quadroni M.;
RL Submitted (JUL-2004) to UniProtKB.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=9724749; DOI=10.1073/pnas.95.18.10596;
RA Berrueta L., Kraeft S.-K., Tirnauer J.S., Schuyler S.C., Chen L.B.,
RA Hill D.E., Pellman D., Bierer B.E.;
RT "The adenomatous polyposis coli-binding protein EB1 is associated with
RT cytoplasmic and spindle microtubules.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10596-10601(1998).
RN [8]
RP INTERACTION WITH DCTN1; DCTN2 AND DYNEIN INTERMEDIATE CHAIN.
RX PubMed=10226031; DOI=10.1016/S0960-9822(99)80190-0;
RA Berrueta L., Tirnauer J.S., Schuyler S.C., Pellman D., Bierer B.E.;
RT "The APC-associated protein EB1 associates with components of the
RT dynactin complex and cytoplasmic dynein intermediate chain.";
RL Curr. Biol. 9:425-428(1999).
RN [9]
RP INTERACTION WITH TUBULIN.
RX PubMed=10188731;
RX DOI=10.1002/(SICI)1097-0215(19990412)81:2<275::AID-IJC18>3.0.CO;2-Z;
RA Juwana J.-P., Henderikx P., Mischo A., Wadle A., Fadle N., Gerlach K.,
RA Arends J.W., Hoogenboom H., Pfreundschuh M., Renner C.;
RT "EB/RP gene family encodes tubulin binding proteins.";
RL Int. J. Cancer 81:275-284(1999).
RN [10]
RP INTERACTION WITH APC2, AND TISSUE SPECIFICITY.
RX PubMed=10644998; DOI=10.1038/sj.onc.1203308;
RA Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.;
RT "EB3, a novel member of the EB1 family preferentially expressed in the
RT central nervous system, binds to a CNS-specific APC homologue.";
RL Oncogene 19:210-216(2000).
RN [11]
RP INTERACTION WITH TERF1.
RX PubMed=11943150; DOI=10.1016/S0014-5793(02)02363-3;
RA Nakamura M., Zhen Zhou X., Kishi S., Ping Lu K.;
RT "Involvement of the telomeric protein Pin2/TRF1 in the regulation of
RT the mitotic spindle.";
RL FEBS Lett. 514:193-198(2002).
RN [12]
RP INTERACTION WITH APC AND DCTN1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=12388762; DOI=10.1091/mbc.E02-01-0061;
RA Askham J.M., Vaughan K.T., Goodson H.V., Morrison E.E.;
RT "Evidence that an interaction between EB1 and p150(Glued) is required
RT for the formation and maintenance of a radial microtubule array
RT anchored at the centrosome.";
RL Mol. Biol. Cell 13:3627-3645(2002).
RN [13]
RP CHARACTERIZATION, AND INTERACTION WITH TUBULIN; APC AND DCTN1.
RX PubMed=14514668; DOI=10.1074/jbc.M306194200;
RA Bu W., Su L.-K.;
RT "Characterization of functional domains of human EB1 family
RT proteins.";
RL J. Biol. Chem. 278:49721-49731(2003).
RN [14]
RP INTERACTION WITH CLASP1 AND CLASP2.
RX PubMed=15631994; DOI=10.1083/jcb.200405094;
RA Mimori-Kiyosue Y., Grigoriev I., Lansbergen G., Sasaki H., Matsui C.,
RA Severin F., Galjart N., Grosveld F., Vorobjev I., Tsukita S.,
RA Akhmanova A.;
RT "CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end
RT dynamics at the cell cortex.";
RL J. Cell Biol. 168:141-153(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [16]
RP INTERACTION WITH CLIP1.
RX PubMed=17563362; DOI=10.1073/pnas.0703876104;
RA Mishima M., Maesaki R., Kasa M., Watanabe T., Fukata M., Kaibuchi K.,
RA Hakoshima T.;
RT "Structural basis for tubulin recognition by cytoplasmic linker
RT protein 170 and its autoinhibition.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10346-10351(2007).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP INTERACTION WITH MTUS2 AND KIF2C.
RX PubMed=19543227; DOI=10.1038/embor.2009.94;
RA Jiang K., Wang J., Liu J., Ward T., Wordeman L., Davidson A., Wang F.,
RA Yao X.;
RT "TIP150 interacts with and targets MCAK at the microtubule plus
RT ends.";
RL EMBO Rep. 10:857-865(2009).
RN [19]
RP INTERACTION WITH MAPRE3.
RX PubMed=19255245; DOI=10.1083/jcb.200807179;
RA Komarova Y., De Groot C.O., Grigoriev I., Gouveia S.M., Munteanu E.L.,
RA Schober J.M., Honnappa S., Buey R.M., Hoogenraad C.C., Dogterom M.,
RA Borisy G.G., Steinmetz M.O., Akhmanova A.;
RT "Mammalian end binding proteins control persistent microtubule
RT growth.";
RL J. Cell Biol. 184:691-706(2009).
RN [20]
RP INTERACTION WITH CDK5RAP2.
RX PubMed=19553473; DOI=10.1091/mbc.E09-01-0009;
RA Fong K.W., Hau S.Y., Kho Y.S., Jia Y., He L., Qi R.Z.;
RT "Interaction of CDK5RAP2 with EB1 to track growing microtubule tips
RT and to regulate microtubule dynamics.";
RL Mol. Biol. Cell 20:3660-3670(2009).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP INTERACTION WITH KIF18B.
RX PubMed=21820309; DOI=10.1016/j.cub.2011.07.017;
RA Tanenbaum M.E., Macurek L., van der Vaart B., Galli M., Akhmanova A.,
RA Medema R.H.;
RT "A complex of Kif18b and MCAK promotes microtubule depolymerization
RT and is negatively regulated by Aurora kinases.";
RL Curr. Biol. 21:1356-1365(2011).
RN [23]
RP INTERACTION WITH SLAIN2 AND CLIP1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21646404; DOI=10.1083/jcb.201012179;
RA van der Vaart B., Manatschal C., Grigoriev I., Olieric V.,
RA Gouveia S.M., Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C.,
RA Steinmetz M.O., Akhmanova A.;
RT "SLAIN2 links microtubule plus end-tracking proteins and controls
RT microtubule growth in interphase.";
RL J. Cell Biol. 193:1083-1099(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP INTERACTION WITH MISP.
RX PubMed=23509069; DOI=10.1083/jcb.201207050;
RA Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L.,
RA Ponting C.P., Goenczy P., Hoffmann I.;
RT "MISP is a novel Plk1 substrate required for proper spindle
RT orientation and mitotic progression.";
RL J. Cell Biol. 200:773-787(2013).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 191-268, DIMERIZATION, AND
RP INTERACTION WITH APC.
RX PubMed=15616574; DOI=10.1038/sj.emboj.7600529;
RA Honnappa S., John C.M., Kostrewa D., Winkler F.K., Steinmetz M.O.;
RT "Structural insights into the EB1-APC interaction.";
RL EMBO J. 24:261-269(2005).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-130, AND MUTAGENESIS OF
RP 59-LYS-LYS-60 AND LYS-89.
RX PubMed=12857735; DOI=10.1074/jbc.M305773200;
RA Hayashi I., Ikura M.;
RT "Crystal structure of the amino-terminal microtubule-binding domain of
RT end-binding protein 1 (EB1).";
RL J. Biol. Chem. 278:36430-36434(2003).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 183-268 IN COMPLEX WITH
RP DCTN1, FUNCTION, SUBUNIT, INTERACTION WITH DCTN1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16109370; DOI=10.1016/j.molcel.2005.06.034;
RA Hayashi I., Wilde A., Mal T.K., Ikura M.;
RT "Structural basis for the activation of microtubule assembly by the
RT EB1 and p150Glued complex.";
RL Mol. Cell 19:449-460(2005).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 191-267 IN COMPLEX WITH
RP DCTN1.
RX PubMed=16949363; DOI=10.1016/j.molcel.2006.07.013;
RA Honnappa S., Okhrimenko O., Jaussi R., Jawhari H., Jelesarov I.,
RA Winkler F.K., Steinmetz M.O.;
RT "Key interaction modes of dynamic +TIP networks.";
RL Mol. Cell 23:663-671(2006).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 12-133.
RX PubMed=17889670; DOI=10.1016/j.molcel.2007.07.023;
RA Slep K.C., Vale R.D.;
RT "Structural basis of microtubule plus end tracking by XMAP215, CLIP-
RT 170, and EB1.";
RL Mol. Cell 27:976-991(2007).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 191-260 IN COMPLEX WITH DST,
RP FUNCTION, INTERACTION WITH APC; CLASP2; KIF2C AND STIM1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19632184; DOI=10.1016/j.cell.2009.04.065;
RA Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S.,
RA Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A.,
RA Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.;
RT "An EB1-binding motif acts as a microtubule tip localization signal.";
RL Cell 138:366-376(2009).
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates the
CC dynamics of the microtubule cytoskeleton. Promotes cytoplasmic
CC microtubule nucleation and elongation. May be involved in spindle
CC function by stabilizing microtubules and anchoring them at
CC centrosomes. May play a role in cell migration.
CC -!- SUBUNIT: Homodimer. Heterodimer with MAPRE3. Interacts with DCTN1,
CC DCTN2, DIAPH1, DIAPH2, TERF1 and dynein intermediate chain.
CC Interacts with APC (via C-terminal domain), CLASP2, DST, KIF2C and
CC STIM1; probably required for their targeting to the growing
CC microtubule plus ends. Interacts with MTUS2; interaction is direct
CC and probably targets MTUS2 to microtubules. Interacts with APC2.
CC Interacts with CLASP1. Interacts with CDK5RAP2. Interacts with
CC MACF1 (By similarity). Interacts with RABL2/RABL2A; binds
CC preferentially to GTP-bound RABL2 (By similarity). Interacts (via
CC C-terminus) with CLIP1. Interacts with SLAIN2. Interacts with
CC KIF18B; this interaction is required for efficient accumulation of
CC KIF18B at microtubule plus ends. Interacts with MISP.
CC -!- INTERACTION:
CC P25054:APC; NbExp=4; IntAct=EBI-1004115, EBI-727707;
CC O95996:APC2; NbExp=3; IntAct=EBI-1004115, EBI-1053045;
CC Q03001:DST; NbExp=2; IntAct=EBI-1004115, EBI-310758;
CC Q99661:KIF2C; NbExp=5; IntAct=EBI-1004115, EBI-1642317;
CC Q5JR59:MTUS2; NbExp=7; IntAct=EBI-1004115, EBI-742948;
CC P54274:TERF1; NbExp=3; IntAct=EBI-1004115, EBI-710997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome.
CC Note=Associated with the microtubule network at the growing distal
CC tip of microtubules. Also enriched at the centrosome.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: Composed of two functionally independent domains. The N-
CC terminal domain forms a hydrophobic cleft involved in microtubule
CC binding and the C-terminal is involved in the formation of
CC mutually exclusive complexes with APC and DCTN1.
CC -!- SIMILARITY: Belongs to the MAPRE family.
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SIMILARITY: Contains 1 EB1 C-terminal domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MAPRE1ID455ch20q11.html";
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DR EMBL; U24166; AAC09471.1; -; mRNA.
DR EMBL; AK312590; BAG35484.1; -; mRNA.
DR EMBL; AL035071; CAB53072.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76348.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76349.1; -; Genomic_DNA.
DR EMBL; BC106068; AAI06069.1; -; mRNA.
DR EMBL; BC109281; AAI09282.1; -; mRNA.
DR PIR; I52726; I52726.
DR RefSeq; NP_036457.1; NM_012325.2.
DR RefSeq; XP_005260394.1; XM_005260337.1.
DR UniGene; Hs.472437; -.
DR PDB; 1PA7; X-ray; 1.45 A; A=1-130.
DR PDB; 1TXQ; X-ray; 1.80 A; B=183-268.
DR PDB; 1UEG; X-ray; 2.40 A; A=1-130.
DR PDB; 1VKA; X-ray; 1.60 A; A/B=2-140.
DR PDB; 1WU9; X-ray; 1.54 A; A/B=191-268.
DR PDB; 1YIB; X-ray; 1.80 A; A=185-254.
DR PDB; 1YIG; X-ray; 2.00 A; A/B=185-254.
DR PDB; 2HKQ; X-ray; 1.86 A; A=191-267.
DR PDB; 2HL3; X-ray; 2.03 A; C=263-268.
DR PDB; 2HL5; X-ray; 1.93 A; A/B=191-267.
DR PDB; 2QJZ; X-ray; 1.25 A; A/B=12-133.
DR PDB; 2R8U; X-ray; 1.35 A; A/B=1-268.
DR PDB; 3GJO; X-ray; 2.50 A; A/B/C/D=191-260.
DR PDB; 3TQ7; X-ray; 2.30 A; A=191-268.
DR PDBsum; 1PA7; -.
DR PDBsum; 1TXQ; -.
DR PDBsum; 1UEG; -.
DR PDBsum; 1VKA; -.
DR PDBsum; 1WU9; -.
DR PDBsum; 1YIB; -.
DR PDBsum; 1YIG; -.
DR PDBsum; 2HKQ; -.
DR PDBsum; 2HL3; -.
DR PDBsum; 2HL5; -.
DR PDBsum; 2QJZ; -.
DR PDBsum; 2R8U; -.
DR PDBsum; 3GJO; -.
DR PDBsum; 3TQ7; -.
DR ProteinModelPortal; Q15691; -.
DR SMR; Q15691; 1-132, 191-257.
DR DIP; DIP-38018N; -.
DR IntAct; Q15691; 19.
DR MINT; MINT-206298; -.
DR STRING; 9606.ENSP00000364721; -.
DR PhosphoSite; Q15691; -.
DR DMDM; 20138589; -.
DR OGP; Q15691; -.
DR REPRODUCTION-2DPAGE; IPI00017596; -.
DR PaxDb; Q15691; -.
DR PeptideAtlas; Q15691; -.
DR PRIDE; Q15691; -.
DR DNASU; 22919; -.
DR Ensembl; ENST00000375571; ENSP00000364721; ENSG00000101367.
DR GeneID; 22919; -.
DR KEGG; hsa:22919; -.
DR UCSC; uc002wyh.3; human.
DR CTD; 22919; -.
DR GeneCards; GC20P031407; -.
DR HGNC; HGNC:6890; MAPRE1.
DR HPA; CAB009337; -.
DR HPA; CAB019391; -.
DR HPA; HPA003600; -.
DR MIM; 603108; gene.
DR neXtProt; NX_Q15691; -.
DR PharmGKB; PA30634; -.
DR eggNOG; COG5217; -.
DR HOGENOM; HOG000198048; -.
DR HOVERGEN; HBG052410; -.
DR InParanoid; Q15691; -.
DR KO; K10436; -.
DR OMA; ATPPNRM; -.
DR OrthoDB; EOG7ZD1W5; -.
DR PhylomeDB; Q15691; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; MAPRE1; human.
DR EvolutionaryTrace; Q15691; -.
DR GeneWiki; MAPRE1; -.
DR GenomeRNAi; 22919; -.
DR NextBio; 43617; -.
DR PRO; PR:Q15691; -.
DR Bgee; Q15691; -.
DR CleanEx; HS_MAPRE1; -.
DR Genevestigator; Q15691; -.
DR GO; GO:0031253; C:cell projection membrane; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0030981; C:cortical microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; IEA:Ensembl.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; TAS:ProtInc.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:UniProtKB.
DR GO; GO:0035372; P:protein localization to microtubule; IDA:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR027739; EB1.
DR InterPro; IPR004953; EB1_C.
DR InterPro; IPR027328; MAPRE.
DR PANTHER; PTHR10623; PTHR10623; 1.
DR PANTHER; PTHR10623:SF8; PTHR10623:SF8; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF03271; EB1; 1.
DR SUPFAM; SSF140612; SSF140612; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51230; EB1_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 268 Microtubule-associated protein RP/EB
FT family member 1.
FT /FTId=PRO_0000213416.
FT DOMAIN 14 116 CH.
FT DOMAIN 185 255 EB1 C-terminal.
FT REGION 124 268 Interaction with MTUS2/TIP150.
FT REGION 185 268 Interaction with CDK5RAP2.
FT REGION 208 268 DCTN1-binding.
FT REGION 220 242 APC-binding.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 124 124 Phosphotyrosine.
FT MUTAGEN 59 60 KK->EE: No effect.
FT MUTAGEN 89 89 K->E: Loss of binding to microtubules.
FT HELIX 17 28
FT HELIX 35 40
FT HELIX 42 51
FT HELIX 58 60
FT HELIX 68 85
FT HELIX 93 96
FT TURN 97 99
FT HELIX 101 118
FT HELIX 126 129
FT HELIX 192 230
FT TURN 231 233
FT HELIX 237 247
FT STRAND 250 252
SQ SEQUENCE 268 AA; 29999 MW; 08C8999F45A145ED CRC64;
MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GAAYCQFMDM LFPGSIALKK
VKFQAKLEHE YIQNFKILQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD
GKDYDPVAAR QGQETAVAPS LVAPALNKPK KPLTSSSAAP QRPISTQRTA AAPKAGPGVV
RKNPGVGNGD DEAAELMQQV NVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ
RIVDILYATD EGFVIPDEGG PQEEQEEY
//
ID MARE1_HUMAN Reviewed; 268 AA.
AC Q15691; B2R6I7; E1P5M8; Q3KQS8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Microtubule-associated protein RP/EB family member 1;
DE AltName: Full=APC-binding protein EB1;
DE AltName: Full=End-binding protein 1;
DE Short=EB1;
GN Name=MAPRE1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH APC.
RX PubMed=7606712;
RA Su L.-K., Burrell M., Hill D.E., Gyuris J., Brent R., Wiltshire R.,
RA Trent J., Vogelstein B., Kinzler K.W.;
RT "APC binds to the novel protein EB1.";
RL Cancer Res. 55:2972-2977(1995).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-17, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V., Potts A., Barblan J., Quadroni M.;
RL Submitted (JUL-2004) to UniProtKB.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=9724749; DOI=10.1073/pnas.95.18.10596;
RA Berrueta L., Kraeft S.-K., Tirnauer J.S., Schuyler S.C., Chen L.B.,
RA Hill D.E., Pellman D., Bierer B.E.;
RT "The adenomatous polyposis coli-binding protein EB1 is associated with
RT cytoplasmic and spindle microtubules.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10596-10601(1998).
RN [8]
RP INTERACTION WITH DCTN1; DCTN2 AND DYNEIN INTERMEDIATE CHAIN.
RX PubMed=10226031; DOI=10.1016/S0960-9822(99)80190-0;
RA Berrueta L., Tirnauer J.S., Schuyler S.C., Pellman D., Bierer B.E.;
RT "The APC-associated protein EB1 associates with components of the
RT dynactin complex and cytoplasmic dynein intermediate chain.";
RL Curr. Biol. 9:425-428(1999).
RN [9]
RP INTERACTION WITH TUBULIN.
RX PubMed=10188731;
RX DOI=10.1002/(SICI)1097-0215(19990412)81:2<275::AID-IJC18>3.0.CO;2-Z;
RA Juwana J.-P., Henderikx P., Mischo A., Wadle A., Fadle N., Gerlach K.,
RA Arends J.W., Hoogenboom H., Pfreundschuh M., Renner C.;
RT "EB/RP gene family encodes tubulin binding proteins.";
RL Int. J. Cancer 81:275-284(1999).
RN [10]
RP INTERACTION WITH APC2, AND TISSUE SPECIFICITY.
RX PubMed=10644998; DOI=10.1038/sj.onc.1203308;
RA Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.;
RT "EB3, a novel member of the EB1 family preferentially expressed in the
RT central nervous system, binds to a CNS-specific APC homologue.";
RL Oncogene 19:210-216(2000).
RN [11]
RP INTERACTION WITH TERF1.
RX PubMed=11943150; DOI=10.1016/S0014-5793(02)02363-3;
RA Nakamura M., Zhen Zhou X., Kishi S., Ping Lu K.;
RT "Involvement of the telomeric protein Pin2/TRF1 in the regulation of
RT the mitotic spindle.";
RL FEBS Lett. 514:193-198(2002).
RN [12]
RP INTERACTION WITH APC AND DCTN1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=12388762; DOI=10.1091/mbc.E02-01-0061;
RA Askham J.M., Vaughan K.T., Goodson H.V., Morrison E.E.;
RT "Evidence that an interaction between EB1 and p150(Glued) is required
RT for the formation and maintenance of a radial microtubule array
RT anchored at the centrosome.";
RL Mol. Biol. Cell 13:3627-3645(2002).
RN [13]
RP CHARACTERIZATION, AND INTERACTION WITH TUBULIN; APC AND DCTN1.
RX PubMed=14514668; DOI=10.1074/jbc.M306194200;
RA Bu W., Su L.-K.;
RT "Characterization of functional domains of human EB1 family
RT proteins.";
RL J. Biol. Chem. 278:49721-49731(2003).
RN [14]
RP INTERACTION WITH CLASP1 AND CLASP2.
RX PubMed=15631994; DOI=10.1083/jcb.200405094;
RA Mimori-Kiyosue Y., Grigoriev I., Lansbergen G., Sasaki H., Matsui C.,
RA Severin F., Galjart N., Grosveld F., Vorobjev I., Tsukita S.,
RA Akhmanova A.;
RT "CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end
RT dynamics at the cell cortex.";
RL J. Cell Biol. 168:141-153(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [16]
RP INTERACTION WITH CLIP1.
RX PubMed=17563362; DOI=10.1073/pnas.0703876104;
RA Mishima M., Maesaki R., Kasa M., Watanabe T., Fukata M., Kaibuchi K.,
RA Hakoshima T.;
RT "Structural basis for tubulin recognition by cytoplasmic linker
RT protein 170 and its autoinhibition.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10346-10351(2007).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP INTERACTION WITH MTUS2 AND KIF2C.
RX PubMed=19543227; DOI=10.1038/embor.2009.94;
RA Jiang K., Wang J., Liu J., Ward T., Wordeman L., Davidson A., Wang F.,
RA Yao X.;
RT "TIP150 interacts with and targets MCAK at the microtubule plus
RT ends.";
RL EMBO Rep. 10:857-865(2009).
RN [19]
RP INTERACTION WITH MAPRE3.
RX PubMed=19255245; DOI=10.1083/jcb.200807179;
RA Komarova Y., De Groot C.O., Grigoriev I., Gouveia S.M., Munteanu E.L.,
RA Schober J.M., Honnappa S., Buey R.M., Hoogenraad C.C., Dogterom M.,
RA Borisy G.G., Steinmetz M.O., Akhmanova A.;
RT "Mammalian end binding proteins control persistent microtubule
RT growth.";
RL J. Cell Biol. 184:691-706(2009).
RN [20]
RP INTERACTION WITH CDK5RAP2.
RX PubMed=19553473; DOI=10.1091/mbc.E09-01-0009;
RA Fong K.W., Hau S.Y., Kho Y.S., Jia Y., He L., Qi R.Z.;
RT "Interaction of CDK5RAP2 with EB1 to track growing microtubule tips
RT and to regulate microtubule dynamics.";
RL Mol. Biol. Cell 20:3660-3670(2009).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP INTERACTION WITH KIF18B.
RX PubMed=21820309; DOI=10.1016/j.cub.2011.07.017;
RA Tanenbaum M.E., Macurek L., van der Vaart B., Galli M., Akhmanova A.,
RA Medema R.H.;
RT "A complex of Kif18b and MCAK promotes microtubule depolymerization
RT and is negatively regulated by Aurora kinases.";
RL Curr. Biol. 21:1356-1365(2011).
RN [23]
RP INTERACTION WITH SLAIN2 AND CLIP1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21646404; DOI=10.1083/jcb.201012179;
RA van der Vaart B., Manatschal C., Grigoriev I., Olieric V.,
RA Gouveia S.M., Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C.,
RA Steinmetz M.O., Akhmanova A.;
RT "SLAIN2 links microtubule plus end-tracking proteins and controls
RT microtubule growth in interphase.";
RL J. Cell Biol. 193:1083-1099(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP INTERACTION WITH MISP.
RX PubMed=23509069; DOI=10.1083/jcb.201207050;
RA Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L.,
RA Ponting C.P., Goenczy P., Hoffmann I.;
RT "MISP is a novel Plk1 substrate required for proper spindle
RT orientation and mitotic progression.";
RL J. Cell Biol. 200:773-787(2013).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 191-268, DIMERIZATION, AND
RP INTERACTION WITH APC.
RX PubMed=15616574; DOI=10.1038/sj.emboj.7600529;
RA Honnappa S., John C.M., Kostrewa D., Winkler F.K., Steinmetz M.O.;
RT "Structural insights into the EB1-APC interaction.";
RL EMBO J. 24:261-269(2005).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-130, AND MUTAGENESIS OF
RP 59-LYS-LYS-60 AND LYS-89.
RX PubMed=12857735; DOI=10.1074/jbc.M305773200;
RA Hayashi I., Ikura M.;
RT "Crystal structure of the amino-terminal microtubule-binding domain of
RT end-binding protein 1 (EB1).";
RL J. Biol. Chem. 278:36430-36434(2003).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 183-268 IN COMPLEX WITH
RP DCTN1, FUNCTION, SUBUNIT, INTERACTION WITH DCTN1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16109370; DOI=10.1016/j.molcel.2005.06.034;
RA Hayashi I., Wilde A., Mal T.K., Ikura M.;
RT "Structural basis for the activation of microtubule assembly by the
RT EB1 and p150Glued complex.";
RL Mol. Cell 19:449-460(2005).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 191-267 IN COMPLEX WITH
RP DCTN1.
RX PubMed=16949363; DOI=10.1016/j.molcel.2006.07.013;
RA Honnappa S., Okhrimenko O., Jaussi R., Jawhari H., Jelesarov I.,
RA Winkler F.K., Steinmetz M.O.;
RT "Key interaction modes of dynamic +TIP networks.";
RL Mol. Cell 23:663-671(2006).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 12-133.
RX PubMed=17889670; DOI=10.1016/j.molcel.2007.07.023;
RA Slep K.C., Vale R.D.;
RT "Structural basis of microtubule plus end tracking by XMAP215, CLIP-
RT 170, and EB1.";
RL Mol. Cell 27:976-991(2007).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 191-260 IN COMPLEX WITH DST,
RP FUNCTION, INTERACTION WITH APC; CLASP2; KIF2C AND STIM1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19632184; DOI=10.1016/j.cell.2009.04.065;
RA Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S.,
RA Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A.,
RA Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.;
RT "An EB1-binding motif acts as a microtubule tip localization signal.";
RL Cell 138:366-376(2009).
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates the
CC dynamics of the microtubule cytoskeleton. Promotes cytoplasmic
CC microtubule nucleation and elongation. May be involved in spindle
CC function by stabilizing microtubules and anchoring them at
CC centrosomes. May play a role in cell migration.
CC -!- SUBUNIT: Homodimer. Heterodimer with MAPRE3. Interacts with DCTN1,
CC DCTN2, DIAPH1, DIAPH2, TERF1 and dynein intermediate chain.
CC Interacts with APC (via C-terminal domain), CLASP2, DST, KIF2C and
CC STIM1; probably required for their targeting to the growing
CC microtubule plus ends. Interacts with MTUS2; interaction is direct
CC and probably targets MTUS2 to microtubules. Interacts with APC2.
CC Interacts with CLASP1. Interacts with CDK5RAP2. Interacts with
CC MACF1 (By similarity). Interacts with RABL2/RABL2A; binds
CC preferentially to GTP-bound RABL2 (By similarity). Interacts (via
CC C-terminus) with CLIP1. Interacts with SLAIN2. Interacts with
CC KIF18B; this interaction is required for efficient accumulation of
CC KIF18B at microtubule plus ends. Interacts with MISP.
CC -!- INTERACTION:
CC P25054:APC; NbExp=4; IntAct=EBI-1004115, EBI-727707;
CC O95996:APC2; NbExp=3; IntAct=EBI-1004115, EBI-1053045;
CC Q03001:DST; NbExp=2; IntAct=EBI-1004115, EBI-310758;
CC Q99661:KIF2C; NbExp=5; IntAct=EBI-1004115, EBI-1642317;
CC Q5JR59:MTUS2; NbExp=7; IntAct=EBI-1004115, EBI-742948;
CC P54274:TERF1; NbExp=3; IntAct=EBI-1004115, EBI-710997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome.
CC Note=Associated with the microtubule network at the growing distal
CC tip of microtubules. Also enriched at the centrosome.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: Composed of two functionally independent domains. The N-
CC terminal domain forms a hydrophobic cleft involved in microtubule
CC binding and the C-terminal is involved in the formation of
CC mutually exclusive complexes with APC and DCTN1.
CC -!- SIMILARITY: Belongs to the MAPRE family.
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SIMILARITY: Contains 1 EB1 C-terminal domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MAPRE1ID455ch20q11.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; U24166; AAC09471.1; -; mRNA.
DR EMBL; AK312590; BAG35484.1; -; mRNA.
DR EMBL; AL035071; CAB53072.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76348.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76349.1; -; Genomic_DNA.
DR EMBL; BC106068; AAI06069.1; -; mRNA.
DR EMBL; BC109281; AAI09282.1; -; mRNA.
DR PIR; I52726; I52726.
DR RefSeq; NP_036457.1; NM_012325.2.
DR RefSeq; XP_005260394.1; XM_005260337.1.
DR UniGene; Hs.472437; -.
DR PDB; 1PA7; X-ray; 1.45 A; A=1-130.
DR PDB; 1TXQ; X-ray; 1.80 A; B=183-268.
DR PDB; 1UEG; X-ray; 2.40 A; A=1-130.
DR PDB; 1VKA; X-ray; 1.60 A; A/B=2-140.
DR PDB; 1WU9; X-ray; 1.54 A; A/B=191-268.
DR PDB; 1YIB; X-ray; 1.80 A; A=185-254.
DR PDB; 1YIG; X-ray; 2.00 A; A/B=185-254.
DR PDB; 2HKQ; X-ray; 1.86 A; A=191-267.
DR PDB; 2HL3; X-ray; 2.03 A; C=263-268.
DR PDB; 2HL5; X-ray; 1.93 A; A/B=191-267.
DR PDB; 2QJZ; X-ray; 1.25 A; A/B=12-133.
DR PDB; 2R8U; X-ray; 1.35 A; A/B=1-268.
DR PDB; 3GJO; X-ray; 2.50 A; A/B/C/D=191-260.
DR PDB; 3TQ7; X-ray; 2.30 A; A=191-268.
DR PDBsum; 1PA7; -.
DR PDBsum; 1TXQ; -.
DR PDBsum; 1UEG; -.
DR PDBsum; 1VKA; -.
DR PDBsum; 1WU9; -.
DR PDBsum; 1YIB; -.
DR PDBsum; 1YIG; -.
DR PDBsum; 2HKQ; -.
DR PDBsum; 2HL3; -.
DR PDBsum; 2HL5; -.
DR PDBsum; 2QJZ; -.
DR PDBsum; 2R8U; -.
DR PDBsum; 3GJO; -.
DR PDBsum; 3TQ7; -.
DR ProteinModelPortal; Q15691; -.
DR SMR; Q15691; 1-132, 191-257.
DR DIP; DIP-38018N; -.
DR IntAct; Q15691; 19.
DR MINT; MINT-206298; -.
DR STRING; 9606.ENSP00000364721; -.
DR PhosphoSite; Q15691; -.
DR DMDM; 20138589; -.
DR OGP; Q15691; -.
DR REPRODUCTION-2DPAGE; IPI00017596; -.
DR PaxDb; Q15691; -.
DR PeptideAtlas; Q15691; -.
DR PRIDE; Q15691; -.
DR DNASU; 22919; -.
DR Ensembl; ENST00000375571; ENSP00000364721; ENSG00000101367.
DR GeneID; 22919; -.
DR KEGG; hsa:22919; -.
DR UCSC; uc002wyh.3; human.
DR CTD; 22919; -.
DR GeneCards; GC20P031407; -.
DR HGNC; HGNC:6890; MAPRE1.
DR HPA; CAB009337; -.
DR HPA; CAB019391; -.
DR HPA; HPA003600; -.
DR MIM; 603108; gene.
DR neXtProt; NX_Q15691; -.
DR PharmGKB; PA30634; -.
DR eggNOG; COG5217; -.
DR HOGENOM; HOG000198048; -.
DR HOVERGEN; HBG052410; -.
DR InParanoid; Q15691; -.
DR KO; K10436; -.
DR OMA; ATPPNRM; -.
DR OrthoDB; EOG7ZD1W5; -.
DR PhylomeDB; Q15691; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; MAPRE1; human.
DR EvolutionaryTrace; Q15691; -.
DR GeneWiki; MAPRE1; -.
DR GenomeRNAi; 22919; -.
DR NextBio; 43617; -.
DR PRO; PR:Q15691; -.
DR Bgee; Q15691; -.
DR CleanEx; HS_MAPRE1; -.
DR Genevestigator; Q15691; -.
DR GO; GO:0031253; C:cell projection membrane; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0030981; C:cortical microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; IEA:Ensembl.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; TAS:ProtInc.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:UniProtKB.
DR GO; GO:0035372; P:protein localization to microtubule; IDA:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR027739; EB1.
DR InterPro; IPR004953; EB1_C.
DR InterPro; IPR027328; MAPRE.
DR PANTHER; PTHR10623; PTHR10623; 1.
DR PANTHER; PTHR10623:SF8; PTHR10623:SF8; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF03271; EB1; 1.
DR SUPFAM; SSF140612; SSF140612; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51230; EB1_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 268 Microtubule-associated protein RP/EB
FT family member 1.
FT /FTId=PRO_0000213416.
FT DOMAIN 14 116 CH.
FT DOMAIN 185 255 EB1 C-terminal.
FT REGION 124 268 Interaction with MTUS2/TIP150.
FT REGION 185 268 Interaction with CDK5RAP2.
FT REGION 208 268 DCTN1-binding.
FT REGION 220 242 APC-binding.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 124 124 Phosphotyrosine.
FT MUTAGEN 59 60 KK->EE: No effect.
FT MUTAGEN 89 89 K->E: Loss of binding to microtubules.
FT HELIX 17 28
FT HELIX 35 40
FT HELIX 42 51
FT HELIX 58 60
FT HELIX 68 85
FT HELIX 93 96
FT TURN 97 99
FT HELIX 101 118
FT HELIX 126 129
FT HELIX 192 230
FT TURN 231 233
FT HELIX 237 247
FT STRAND 250 252
SQ SEQUENCE 268 AA; 29999 MW; 08C8999F45A145ED CRC64;
MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GAAYCQFMDM LFPGSIALKK
VKFQAKLEHE YIQNFKILQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD
GKDYDPVAAR QGQETAVAPS LVAPALNKPK KPLTSSSAAP QRPISTQRTA AAPKAGPGVV
RKNPGVGNGD DEAAELMQQV NVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ
RIVDILYATD EGFVIPDEGG PQEEQEEY
//
MIM
603108
*RECORD*
*FIELD* NO
603108
*FIELD* TI
*603108 MICROTUBULE-ASSOCIATED PROTEIN, RP/EB FAMILY, MEMBER 1; MAPRE1
;;END-BINDING PROTEIN 1; EB1;;
read moreADENOMATOUS POLYPOSIS COLI-BINDING PROTEIN EB1
*FIELD* TX
DESCRIPTION
MAPRE1 is a regulator of microtubule dynamics that localizes at both the
growing plus ends of microtubules and the centrosome. It is involved in
a variety of cellular processes, including establishment and maintenance
of cell polarity, search and capture of chromosomes during mitosis, and
positioning of the mitotic spindle during asymmetric cell division (Sun
et al., 2008).
CLONING
EB1 is a 30- to 35-kD protein that was isolated in a yeast 2-hybrid
screen by its binding to the C-terminal domain of APC (611731) (Su et
al., 1995), a domain that is deleted in the majority of familial and
sporadic forms of colon carcinoma.
GENE FAMILY
By genomic sequence analysis, Su and Qi (2001) showed that there are
most likely 3 MAPRE genes: MAPRE1, which encodes EB1, MAPRE2 (605789),
which encodes RP1 and the EB2 fragment, and MAPRE3 (605788), which
encodes EBF3 and the fragment RP3.
GENE FUNCTION
Berrueta et al. (1998) undertook a systematic study of EB1 subcellular
localization during cell cycle, using both biochemical and
immunofluorescence techniques. Using monoclonal antibodies specific for
EB1, they demonstrated that EB1 decorated part of the microtubule
cytoskeleton during interphase, with pronounced staining of the
centrosome. During cell division, EB1 localized to the mitotic
apparatus. This microtubule localization was abolished in the presence
of the microtubule-destabilizing drug nocodazole; upon drug removal, the
microtubule distribution of EB1 was recovered and EB1 fluorescence
concentrated at the microtubule-organizing center. These results
suggested that EB1 is associated with the microtubule network and may be
involved in microtubule polymerization and spindle function. Associating
with the mitotic apparatus, EB1 may play a physiologic role connecting
APC to cell division, coordinating the control of normal growth and
differentiation processes in the colonic epithelium.
Tirnauer and Bierer (2000) reviewed the biology of EB1 family proteins.
They noted that EB1 is a microtubule end-binding protein and that EB1
coimmunoprecipitates the dynactin components p150(GLUED) (DCTN1;
601143), p50/dynamitin (DCTN2; 607376), and the intermediate chain of
dynein (see DNCI2; 603331) from lymphocytes and epithelial cells
(Berrueta et al., 1999).
By yeast 2-hybrid analysis of a HeLa cell cDNA library and pull-down
assays using recombinant proteins, Sun et al. (2008) showed that the
C-terminal tail of EB1 interacted specifically with the catalytic domain
of Aurora kinase B (AURKB; 604970). The proteins colocalized on the
central spindle in anaphase and in the midbody during cytokinesis in
simian kidney cells, and endogenous EB1 and AURKB coimmunoprecipitated
from HeLa cells. EB1 overexpression enhanced AURKB kinase activity, and
knockdown of EB1 with small interfering RNA impaired AURKB activity. EB1
protected AURKB from dephosphorylation/inactivation by protein
phosphatase-2A (PP2A; see 176915) by blocking binding of PP2A to AURKB.
Sun et al. (2008) concluded that EB1 stimulates AURKB activity by
antagonizing its dephosphorylation/inactivation by PP2A.
Using U2OS human osteosarcoma cells, Tanenbaum et al. (2011) identified
KIF18B (614570) as an essential component of a
microtubule-depolymerizing complex containing MCAK (KIF2C; 604538) and
EB1. KIF18B interacted independently with MCAK and a subset of EB1 at
microtubule plus ends. All 3 proteins, in addition to KIF18B motor
activity, were required for efficient plus-end microtubule
depolymerization. Knockdown of either KIF18B or MCAK reduced the
localization of the other protein at microtubule plus ends and reduced
microtubule depolymerization. Disruption of the MCAK-KIF18B interaction
by mutation of the interacting domains, or phosphorylation of MCAK by
the microtubule-polymerizing agents Aurora A (AURKA; 603072) or Aurora
B, similarly blocked microtubule depolymerization. Use of a KIF5B
(602809)/KIF18B chimera revealed that the major role of KIF18B motor
domain in this process was to provide plus end-directed movement along
microtubules. Tanenbaum et al. (2011) hypothesized that KIF18B, released
into the cytoplasm upon mitotic nuclear envelope breakdown, is recruited
to microtubule plus ends through interaction with EB1 and MCAK. The
motor activity of KIF18B directs the complex to the tip of microtubules,
and the depolymerizing activity of the complex is modulated by Aurora A
and Aurora B.
GENE STRUCTURE
Su and Qi (2001) determined that MAPRE1, like MAPRE2 and MAPRE3,
contains 7 exons. However, the coding region of MAPRE1 spans more than
22 kb due to its long introns.
MAPPING
Using FISH, Su et al. (1995) mapped the MAPRE1 gene to chromosome
20q11.2. Su and Qi (2001) confirmed this localization by identifying
MAPRE1 in a genomic clone from chromosome 20q11.1-q11.23.
*FIELD* RF
1. Berrueta, L.; Kraeft, S.-K.; Tirnauer, J. S.; Schuyler, S. C.;
Chen, L. B.; Hill, D. E.; Pellman, D.; Bierer, B. E.: The adenomatous
polyposis coli-binding protein EB1 is associated with cytoplasmic
and spindle microtubules. Proc. Nat. Acad. Sci. 95: 10596-10601,
1998.
2. Berrueta, L.; Tirnauer, J. S.; Schuyler, S. C.; Pellman, D.; Bierer,
B. E.: The APC-associated protein EB1 associates with components
of the dynactin complex and cytoplasmic dynein intermediate chain. Curr.
Biol. 9: 425-428, 1999.
3. Su, L.-K.; Burrell, M.; Hill, D. E.; Gyuris, J.; Brent, R.; Wiltshire,
R.; Trent, J.; Vogelstein, B.; Kinzler, K. W.: APC binds to the novel
protein EB1. Cancer Res. 55: 2972-2977, 1995.
4. Su, L.-K.; Burrell, M.; Hill, D. E.; Gyuris, J.; Brent, R.; Wiltshire,
R.; Trent, J.; Vogelstein, B.; Kinzler, K. W.: APC binds to the novel
protein EB1. Cancer Res. 55: 2972-2977, 1995.
5. Su, L.-K.; Qi, Y.: Characterization of human MAPRE genes and their
proteins. Genomics 71: 143-149, 2001.
6. Sun, L.; Gao, J.; Dong, X.; Liu, M.; Li, D.; Shi, X.; Dong, J.-T.;
Lu, X.; Liu, C.: EB1 promotes Aurora-B kinase activity through blocking
its inactivation by protein phosphatase 2A. Proc. Nat. Acad. Sci. 105:
7153-7158, 2008. Note: Erratum: Proc. Nat. Acad. Sci. 105: 9129 only,
2008.
7. Tanenbaum, M. E.; Macurek, L.; van der Vaart, B.; Galli, M.; Akhmanova,
A.; Medema, R. H.: A complex of Kif18b and MCAK promotes microtubule
depolymerization and is negatively regulated by Aurora kinases. Curr.
Biol. 21: 1356-1365, 2011.
8. Tirnauer, J. S.; Bierer, B. E.: EB1 proteins regulate microtubule
dynamics, cell polarity, and chromosome stability. J. Cell Biol. 149:
761-766, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 4/13/2012
Patricia A. Hartz - updated: 7/23/2008
Paul J. Converse - updated: 3/28/2001
Paul J. Converse - updated: 8/21/2000
*FIELD* CD
Victor A. McKusick: 10/9/1998
*FIELD* ED
terry: 10/02/2012
mgross: 4/13/2012
mgross: 7/23/2008
ckniffin: 2/5/2008
mgross: 11/22/2002
mgross: 3/29/2001
mgross: 3/28/2001
mgross: 8/21/2000
carol: 12/10/1999
carol: 10/9/1998
*RECORD*
*FIELD* NO
603108
*FIELD* TI
*603108 MICROTUBULE-ASSOCIATED PROTEIN, RP/EB FAMILY, MEMBER 1; MAPRE1
;;END-BINDING PROTEIN 1; EB1;;
read moreADENOMATOUS POLYPOSIS COLI-BINDING PROTEIN EB1
*FIELD* TX
DESCRIPTION
MAPRE1 is a regulator of microtubule dynamics that localizes at both the
growing plus ends of microtubules and the centrosome. It is involved in
a variety of cellular processes, including establishment and maintenance
of cell polarity, search and capture of chromosomes during mitosis, and
positioning of the mitotic spindle during asymmetric cell division (Sun
et al., 2008).
CLONING
EB1 is a 30- to 35-kD protein that was isolated in a yeast 2-hybrid
screen by its binding to the C-terminal domain of APC (611731) (Su et
al., 1995), a domain that is deleted in the majority of familial and
sporadic forms of colon carcinoma.
GENE FAMILY
By genomic sequence analysis, Su and Qi (2001) showed that there are
most likely 3 MAPRE genes: MAPRE1, which encodes EB1, MAPRE2 (605789),
which encodes RP1 and the EB2 fragment, and MAPRE3 (605788), which
encodes EBF3 and the fragment RP3.
GENE FUNCTION
Berrueta et al. (1998) undertook a systematic study of EB1 subcellular
localization during cell cycle, using both biochemical and
immunofluorescence techniques. Using monoclonal antibodies specific for
EB1, they demonstrated that EB1 decorated part of the microtubule
cytoskeleton during interphase, with pronounced staining of the
centrosome. During cell division, EB1 localized to the mitotic
apparatus. This microtubule localization was abolished in the presence
of the microtubule-destabilizing drug nocodazole; upon drug removal, the
microtubule distribution of EB1 was recovered and EB1 fluorescence
concentrated at the microtubule-organizing center. These results
suggested that EB1 is associated with the microtubule network and may be
involved in microtubule polymerization and spindle function. Associating
with the mitotic apparatus, EB1 may play a physiologic role connecting
APC to cell division, coordinating the control of normal growth and
differentiation processes in the colonic epithelium.
Tirnauer and Bierer (2000) reviewed the biology of EB1 family proteins.
They noted that EB1 is a microtubule end-binding protein and that EB1
coimmunoprecipitates the dynactin components p150(GLUED) (DCTN1;
601143), p50/dynamitin (DCTN2; 607376), and the intermediate chain of
dynein (see DNCI2; 603331) from lymphocytes and epithelial cells
(Berrueta et al., 1999).
By yeast 2-hybrid analysis of a HeLa cell cDNA library and pull-down
assays using recombinant proteins, Sun et al. (2008) showed that the
C-terminal tail of EB1 interacted specifically with the catalytic domain
of Aurora kinase B (AURKB; 604970). The proteins colocalized on the
central spindle in anaphase and in the midbody during cytokinesis in
simian kidney cells, and endogenous EB1 and AURKB coimmunoprecipitated
from HeLa cells. EB1 overexpression enhanced AURKB kinase activity, and
knockdown of EB1 with small interfering RNA impaired AURKB activity. EB1
protected AURKB from dephosphorylation/inactivation by protein
phosphatase-2A (PP2A; see 176915) by blocking binding of PP2A to AURKB.
Sun et al. (2008) concluded that EB1 stimulates AURKB activity by
antagonizing its dephosphorylation/inactivation by PP2A.
Using U2OS human osteosarcoma cells, Tanenbaum et al. (2011) identified
KIF18B (614570) as an essential component of a
microtubule-depolymerizing complex containing MCAK (KIF2C; 604538) and
EB1. KIF18B interacted independently with MCAK and a subset of EB1 at
microtubule plus ends. All 3 proteins, in addition to KIF18B motor
activity, were required for efficient plus-end microtubule
depolymerization. Knockdown of either KIF18B or MCAK reduced the
localization of the other protein at microtubule plus ends and reduced
microtubule depolymerization. Disruption of the MCAK-KIF18B interaction
by mutation of the interacting domains, or phosphorylation of MCAK by
the microtubule-polymerizing agents Aurora A (AURKA; 603072) or Aurora
B, similarly blocked microtubule depolymerization. Use of a KIF5B
(602809)/KIF18B chimera revealed that the major role of KIF18B motor
domain in this process was to provide plus end-directed movement along
microtubules. Tanenbaum et al. (2011) hypothesized that KIF18B, released
into the cytoplasm upon mitotic nuclear envelope breakdown, is recruited
to microtubule plus ends through interaction with EB1 and MCAK. The
motor activity of KIF18B directs the complex to the tip of microtubules,
and the depolymerizing activity of the complex is modulated by Aurora A
and Aurora B.
GENE STRUCTURE
Su and Qi (2001) determined that MAPRE1, like MAPRE2 and MAPRE3,
contains 7 exons. However, the coding region of MAPRE1 spans more than
22 kb due to its long introns.
MAPPING
Using FISH, Su et al. (1995) mapped the MAPRE1 gene to chromosome
20q11.2. Su and Qi (2001) confirmed this localization by identifying
MAPRE1 in a genomic clone from chromosome 20q11.1-q11.23.
*FIELD* RF
1. Berrueta, L.; Kraeft, S.-K.; Tirnauer, J. S.; Schuyler, S. C.;
Chen, L. B.; Hill, D. E.; Pellman, D.; Bierer, B. E.: The adenomatous
polyposis coli-binding protein EB1 is associated with cytoplasmic
and spindle microtubules. Proc. Nat. Acad. Sci. 95: 10596-10601,
1998.
2. Berrueta, L.; Tirnauer, J. S.; Schuyler, S. C.; Pellman, D.; Bierer,
B. E.: The APC-associated protein EB1 associates with components
of the dynactin complex and cytoplasmic dynein intermediate chain. Curr.
Biol. 9: 425-428, 1999.
3. Su, L.-K.; Burrell, M.; Hill, D. E.; Gyuris, J.; Brent, R.; Wiltshire,
R.; Trent, J.; Vogelstein, B.; Kinzler, K. W.: APC binds to the novel
protein EB1. Cancer Res. 55: 2972-2977, 1995.
4. Su, L.-K.; Burrell, M.; Hill, D. E.; Gyuris, J.; Brent, R.; Wiltshire,
R.; Trent, J.; Vogelstein, B.; Kinzler, K. W.: APC binds to the novel
protein EB1. Cancer Res. 55: 2972-2977, 1995.
5. Su, L.-K.; Qi, Y.: Characterization of human MAPRE genes and their
proteins. Genomics 71: 143-149, 2001.
6. Sun, L.; Gao, J.; Dong, X.; Liu, M.; Li, D.; Shi, X.; Dong, J.-T.;
Lu, X.; Liu, C.: EB1 promotes Aurora-B kinase activity through blocking
its inactivation by protein phosphatase 2A. Proc. Nat. Acad. Sci. 105:
7153-7158, 2008. Note: Erratum: Proc. Nat. Acad. Sci. 105: 9129 only,
2008.
7. Tanenbaum, M. E.; Macurek, L.; van der Vaart, B.; Galli, M.; Akhmanova,
A.; Medema, R. H.: A complex of Kif18b and MCAK promotes microtubule
depolymerization and is negatively regulated by Aurora kinases. Curr.
Biol. 21: 1356-1365, 2011.
8. Tirnauer, J. S.; Bierer, B. E.: EB1 proteins regulate microtubule
dynamics, cell polarity, and chromosome stability. J. Cell Biol. 149:
761-766, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 4/13/2012
Patricia A. Hartz - updated: 7/23/2008
Paul J. Converse - updated: 3/28/2001
Paul J. Converse - updated: 8/21/2000
*FIELD* CD
Victor A. McKusick: 10/9/1998
*FIELD* ED
terry: 10/02/2012
mgross: 4/13/2012
mgross: 7/23/2008
ckniffin: 2/5/2008
mgross: 11/22/2002
mgross: 3/29/2001
mgross: 3/28/2001
mgross: 8/21/2000
carol: 12/10/1999
carol: 10/9/1998