MARE1_HUMAN
ID MARE1_HUMAN Reviewed; 268 AA.
AC Q15691; B2R6I7; E1P5M8; Q3KQS8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 224.
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 {ECO:0000303|PubMed:7606712};
DE Short=EB1 {ECO:0000303|PubMed:7606712};
GN Name=MAPRE1 {ECO:0000312|HGNC:HGNC:6890};
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], 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., 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., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [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 project:
RT 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 IDENTIFICATION BY MASS
RP 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 dynactin
RT complex and cytoplasmic dynein intermediate chain.";
RL Curr. Biol. 9:425-428(1999).
RN [9]
RP INTERACTION WITH TUBULIN, AND SUBCELLULAR LOCATION.
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 the
RT 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 for
RT the formation and maintenance of a radial microtubule array anchored at the
RT 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 proteins.";
RL J. Biol. Chem. 278:49721-49731(2003).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [15]
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., Akhmanova A.;
RT "CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics
RT at the cell cortex.";
RL J. Cell Biol. 168:141-153(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [17]
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 protein 170
RT and its autoinhibition.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10346-10351(2007).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
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 ends.";
RL EMBO Rep. 10:857-865(2009).
RN [20]
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 growth.";
RL J. Cell Biol. 184:691-706(2009).
RN [21]
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 and to
RT regulate microtubule dynamics.";
RL Mol. Biol. Cell 20:3660-3670(2009).
RN [22]
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., Buerckstuemmer T.,
RA 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 [23]
RP INTERACTION WITH RARRES1 AND AGBL2.
RX PubMed=21303978; DOI=10.1158/0008-5472.can-10-2294;
RA Sahab Z.J., Hall M.D., Me Sung Y., Dakshanamurthy S., Ji Y., Kumar D.,
RA Byers S.W.;
RT "Tumor suppressor RARRES1 interacts with cytoplasmic carboxypeptidase AGBL2
RT to regulate the alpha-tubulin tyrosination cycle.";
RL Cancer Res. 71:1219-1228(2011).
RN [24]
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 and is
RT negatively regulated by Aurora kinases.";
RL Curr. Biol. 21:1356-1365(2011).
RN [25]
RP FUNCTION, INTERACTION WITH SLAIN2; SLAIN1 AND CLIP1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21646404; DOI=10.1083/jcb.201012179;
RA van der Vaart B., Manatschal C., Grigoriev I., Olieric V., Gouveia S.M.,
RA Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C., Steinmetz M.O.,
RA 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 [26]
RP INTERACTION WITH KNSTRN.
RX PubMed=23035123; DOI=10.1074/jbc.m112.406652;
RA Wang X., Zhuang X., Cao D., Chu Y., Yao P., Liu W., Liu L., Adams G.,
RA Fang G., Dou Z., Ding X., Huang Y., Wang D., Yao X.;
RT "Mitotic regulator SKAP forms a link between kinetochore core complex KMN
RT and dynamic spindle microtubules.";
RL J. Biol. Chem. 287:39380-39390(2012).
RN [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [29]
RP FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-220, AND MUTAGENESIS OF
RP LYS-220.
RX PubMed=23001180; DOI=10.1073/pnas.1202639109;
RA Xia P., Wang Z., Liu X., Wu B., Wang J., Ward T., Zhang L., Ding X.,
RA Gibbons G., Shi Y., Yao X.;
RT "EB1 acetylation by P300/CBP-associated factor (PCAF) ensures accurate
RT kinetochore-microtubule interactions in mitosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:16564-16569(2012).
RN [30]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MISP.
RX PubMed=23509069; DOI=10.1083/jcb.201207050;
RA Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P.,
RA Goenczy P., Hoffmann I.;
RT "MISP is a novel Plk1 substrate required for proper spindle orientation and
RT mitotic progression.";
RL J. Cell Biol. 200:773-787(2013).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [32]
RP INTERACTION WITH DCTN1.
RX PubMed=23874158; DOI=10.1371/journal.pbio.1001611;
RA Lazarus J.E., Moughamian A.J., Tokito M.K., Holzbaur E.L.;
RT "Dynactin subunit p150(Glued) is a neuron-specific anti-catastrophe
RT factor.";
RL PLoS Biol. 11:E1001611-E1001611(2013).
RN [33]
RP INTERACTION WITH GAS2L1; GAS2L2 AND GAS2L3.
RX PubMed=24706950; DOI=10.1242/jcs.140558;
RA Stroud M.J., Nazgiewicz A., McKenzie E.A., Wang Y., Kammerer R.A.,
RA Ballestrem C.;
RT "GAS2-like proteins mediate communication between microtubules and actin
RT through interactions with end-binding proteins.";
RL J. Cell Sci. 127:2672-2682(2014).
RN [34]
RP INTERACTION WITH PDE4DIP, AND SUBCELLULAR LOCATION.
RX PubMed=25217626; DOI=10.1242/jcs.155408;
RA Wang Z., Zhang C., Qi R.Z.;
RT "A newly identified myomegalin isoform functions in Golgi microtubule
RT organization and ER-Golgi transport.";
RL J. Cell Sci. 127:4904-4917(2014).
RN [35]
RP IDENTIFICATION BY 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 [36]
RP INTERACTION WITH NCKAP5L.
RX PubMed=26485573; DOI=10.1371/journal.pone.0140968;
RA Mori Y., Inoue Y., Tanaka S., Doda S., Yamanaka S., Fukuchi H., Terada Y.;
RT "Cep169, a novel microtubule plus-end-tracking centrosomal protein, binds
RT to CDK5RAP2 and regulates microtubule stability.";
RL PLoS ONE 10:E0140968-E0140968(2015).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [38]
RP FUNCTION, AND INTERACTION WITH CAMSAP2.
RX PubMed=28726242; DOI=10.1002/1873-3468.12758;
RA Wei J., Xu H., Meng W.;
RT "Noncentrosomal microtubules regulate autophagosome transport through
RT CAMSAP2-EB1 cross-talk.";
RL FEBS Lett. 591:2379-2393(2017).
RN [39]
RP FUNCTION, AND INTERACTION WITH AKAP9 AND PDE4DIP.
RX PubMed=28814570; DOI=10.1083/jcb.201701024;
RA Yang C., Wu J., de Heus C., Grigoriev I., Liv N., Yao Y., Smal I.,
RA Meijering E., Klumperman J., Qi R.Z., Akhmanova A.;
RT "EB1 and EB3 regulate microtubule minus end organization and Golgi
RT morphology.";
RL J. Cell Biol. 216:3179-3198(2017).
RN [40]
RP INTERACTION WITH AKAP9; CDK5RAP2 AND PDE4DIP.
RX PubMed=29162697; DOI=10.1073/pnas.1705682114;
RA Bouguenina H., Salaun D., Mangon A., Muller L., Baudelet E., Camoin L.,
RA Tachibana T., Cianferani S., Audebert S., Verdier-Pinard P., Badache A.;
RT "EB1-binding-myomegalin protein complex promotes centrosomal microtubules
RT functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E10687-E10696(2017).
RN [41]
RP FUNCTION, SUBCELLULAR LOCATION, CROTONYLATION AT LYS-66, AND MUTAGENESIS OF
RP LYS-66.
RX PubMed=34608293; DOI=10.1038/s41589-021-00875-7;
RA Song X., Yang F., Liu X., Xia P., Yin W., Wang Z., Wang Y., Yuan X.,
RA Dou Z., Jiang K., Ma M., Hu B., Zhang R., Xu C., Zhang Z., Ruan K.,
RA Tian R., Li L., Liu T., Hill D.L., Zang J., Liu X., Li J., Cheng J.,
RA Yao X.;
RT "Dynamic crotonylation of EB1 by TIP60 ensures accurate spindle positioning
RT in mitosis.";
RL Nat. Chem. Biol. 17:1314-1323(2021).
RN [42]
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 [43]
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 end-
RT binding protein 1 (EB1).";
RL J. Biol. Chem. 278:36430-36434(2003).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 183-268 IN COMPLEX WITH DCTN1,
RP FUNCTION, SUBUNIT, INTERACTION WITH DCTN1, AND SUBCELLULAR 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 EB1 and
RT p150Glued complex.";
RL Mol. Cell 19:449-460(2005).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 191-267 IN COMPLEX WITH 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 [46]
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-170,
RT and EB1.";
RL Mol. Cell 27:976-991(2007).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 191-260 IN COMPLEX WITH DST,
RP FUNCTION, INTERACTION WITH APC; CLASP2; KIF2C AND STIM1, AND SUBCELLULAR
RP 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: Plus-end tracking protein (+TIP) that binds to the plus-end
CC of microtubules and regulates the dynamics of the microtubule
CC cytoskeleton (PubMed:12388762, PubMed:16109370, PubMed:19632184,
CC PubMed:21646404, PubMed:23001180, PubMed:28726242, PubMed:28814570,
CC PubMed:34608293). Promotes cytoplasmic microtubule nucleation and
CC elongation (PubMed:12388762, PubMed:16109370, PubMed:19632184,
CC PubMed:21646404, PubMed:28726242, PubMed:28814570). Involved in mitotic
CC spindle positioning by stabilizing microtubules and promoting dynamic
CC connection between astral microtubules and the cortex during mitotic
CC chromosome segregation (PubMed:12388762, PubMed:34608293). Also acts as
CC a regulator of minus-end microtubule organization: interacts with the
CC complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the
CC Golgi apparatus, thereby tethering non-centrosomal minus-end
CC microtubules to the Golgi, an important step for polarized cell
CC movement (PubMed:28814570). Promotes elongation of CAMSAP2-decorated
CC microtubule stretches on the minus-end of microtubules
CC (PubMed:28814570). Acts as a regulator of autophagosome transport via
CC interaction with CAMSAP2 (PubMed:28726242). May play a role in cell
CC migration (By similarity). {ECO:0000250|UniProtKB:Q61166,
CC ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:16109370,
CC ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21646404,
CC ECO:0000269|PubMed:23001180, ECO:0000269|PubMed:28726242,
CC ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:34608293}.
CC -!- SUBUNIT: Homodimer (PubMed:15616574). Heterodimer with MAPRE3
CC (PubMed:19255245). Interacts with DCTN1, DCTN2, TERF1 and dynein
CC intermediate chain (PubMed:10226031, PubMed:11943150, PubMed:12388762,
CC PubMed:14514668, PubMed:23874158, PubMed:16109370, PubMed:16949363).
CC Interaction with DIAPH1 and DIAPH2 (By similarity). Interacts with APC
CC (via C-terminal domain), CLASP2, DST, KIF2C and STIM1; probably
CC required for their targeting to the growing microtubule plus ends
CC (PubMed:7606712, PubMed:12388762, PubMed:14514668, PubMed:15631994,
CC PubMed:19543227, PubMed:15616574, PubMed:19632184). Interacts with
CC MTUS2; interaction is direct and probably targets MTUS2 to microtubules
CC (PubMed:19543227). Interacts with APC2 (PubMed:10644998). Interacts
CC with CLASP1 (PubMed:15631994). Interacts with CDK5RAP2
CC (PubMed:19553473). Interacts with MACF1 (By similarity). Interacts with
CC RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (By similarity).
CC Interacts with KCNAB2 (By similarity). Interacts (via C-terminus) with
CC CLIP1 (PubMed:17563362, PubMed:21646404). Interacts with SLAIN2 and
CC SLAIN1 (PubMed:21646404). Interacts with KIF18B; this interaction is
CC required for efficient accumulation of KIF18B at microtubule plus ends
CC (PubMed:21820309). Interacts with MISP (PubMed:23509069). Interacts
CC with KNSTRN (PubMed:23035123). Interacts with NCKAP5L
CC (PubMed:26485573). Interacts with CAMSAP2 (PubMed:28726242). Interacts
CC with PDE4DIP isoform 13/MMG8/SMYLE; this interaction is required for
CC its recruitment to the Golgi apparatus (PubMed:25217626,
CC PubMed:28814570). Forms a pericentrosomal complex with AKAP9, CDK5RAP2
CC and PDE4DIP isoform 13/MMG8/SMYLE; within this complex, MAPRE1 binding
CC to CDK5RAP2 may be mediated by PDE4DIP (PubMed:29162697). Interacts
CC with AKNA (By similarity). Interacts with GAS2L1, GAS2L2, and GAS2L3
CC (PubMed:24706950). Interacts with RARRES1 and AGBL2 (PubMed:21303978).
CC {ECO:0000250|UniProtKB:Q61166, ECO:0000269|PubMed:10226031,
CC ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:11943150,
CC ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:14514668,
CC ECO:0000269|PubMed:15616574, ECO:0000269|PubMed:15631994,
CC ECO:0000269|PubMed:16109370, ECO:0000269|PubMed:16949363,
CC ECO:0000269|PubMed:17563362, ECO:0000269|PubMed:19255245,
CC ECO:0000269|PubMed:19543227, ECO:0000269|PubMed:19553473,
CC ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21303978,
CC ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:21820309,
CC ECO:0000269|PubMed:23035123, ECO:0000269|PubMed:23509069,
CC ECO:0000269|PubMed:23874158, ECO:0000269|PubMed:24706950,
CC ECO:0000269|PubMed:25217626, ECO:0000269|PubMed:26485573,
CC ECO:0000269|PubMed:28726242, ECO:0000269|PubMed:28814570,
CC ECO:0000269|PubMed:29162697, ECO:0000269|PubMed:7606712}.
CC -!- INTERACTION:
CC Q15691; P25054: APC; NbExp=5; IntAct=EBI-1004115, EBI-727707;
CC Q15691; O95996: APC2; NbExp=3; IntAct=EBI-1004115, EBI-1053045;
CC Q15691; Q96GD4: AURKB; NbExp=5; IntAct=EBI-1004115, EBI-624291;
CC Q15691; A1L168: C20orf202; NbExp=3; IntAct=EBI-1004115, EBI-18396958;
CC Q15691; Q9C0I3-2: CCSER1; NbExp=3; IntAct=EBI-1004115, EBI-17793327;
CC Q15691; O75122: CLASP2; NbExp=3; IntAct=EBI-1004115, EBI-913524;
CC Q15691; P30622: CLIP1; NbExp=2; IntAct=EBI-1004115, EBI-2683569;
CC Q15691; P30622-1: CLIP1; NbExp=2; IntAct=EBI-1004115, EBI-9640673;
CC Q15691; P30622-2: CLIP1; NbExp=4; IntAct=EBI-1004115, EBI-6479976;
CC Q15691; Q14203: DCTN1; NbExp=7; IntAct=EBI-1004115, EBI-724352;
CC Q15691; P15924: DSP; NbExp=7; IntAct=EBI-1004115, EBI-355041;
CC Q15691; Q03001: DST; NbExp=4; IntAct=EBI-1004115, EBI-310758;
CC Q15691; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-1004115, EBI-7960826;
CC Q15691; Q99661: KIF2C; NbExp=7; IntAct=EBI-1004115, EBI-1642317;
CC Q15691; Q53G59: KLHL12; NbExp=3; IntAct=EBI-1004115, EBI-740929;
CC Q15691; Q9Y448: KNSTRN; NbExp=4; IntAct=EBI-1004115, EBI-373334;
CC Q15691; P25791: LMO2; NbExp=6; IntAct=EBI-1004115, EBI-739696;
CC Q15691; P25791-3: LMO2; NbExp=6; IntAct=EBI-1004115, EBI-11959475;
CC Q15691; Q15691: MAPRE1; NbExp=8; IntAct=EBI-1004115, EBI-1004115;
CC Q15691; Q15555: MAPRE2; NbExp=8; IntAct=EBI-1004115, EBI-739717;
CC Q15691; Q9UPY8: MAPRE3; NbExp=19; IntAct=EBI-1004115, EBI-726739;
CC Q15691; Q9H992: MARCHF7; NbExp=3; IntAct=EBI-1004115, EBI-949983;
CC Q15691; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1004115, EBI-16439278;
CC Q15691; Q5JR59: MTUS2; NbExp=7; IntAct=EBI-1004115, EBI-742948;
CC Q15691; P26367: PAX6; NbExp=3; IntAct=EBI-1004115, EBI-747278;
CC Q15691; Q5VU43: PDE4DIP; NbExp=5; IntAct=EBI-1004115, EBI-1105124;
CC Q15691; P56282: POLE2; NbExp=6; IntAct=EBI-1004115, EBI-713847;
CC Q15691; O60828: PQBP1; NbExp=6; IntAct=EBI-1004115, EBI-713867;
CC Q15691; P25786: PSMA1; NbExp=6; IntAct=EBI-1004115, EBI-359352;
CC Q15691; Q495Y8: SPDYE2; NbExp=3; IntAct=EBI-1004115, EBI-10241662;
CC Q15691; P0CI01: SPDYE6; NbExp=3; IntAct=EBI-1004115, EBI-11960469;
CC Q15691; P54274: TERF1; NbExp=2; IntAct=EBI-1004115, EBI-710997;
CC Q15691; Q12815: TROAP; NbExp=9; IntAct=EBI-1004115, EBI-2349743;
CC Q15691; Q96CK0: ZNF653; NbExp=3; IntAct=EBI-1004115, EBI-12217757;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10188731, ECO:0000269|PubMed:12388762,
CC ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:23001180,
CC ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:9724749}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:14654843}. Golgi
CC apparatus {ECO:0000269|PubMed:25217626}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000269|PubMed:23509069}. Cytoplasm, cytoskeleton, spindle
CC pole {ECO:0000269|PubMed:34608293}. Note=Associated with the
CC microtubule growing distal tips (PubMed:28814570). Recruitment to the
CC Golgi apparatus requires the presence of PDE4DIP isoform 13/MMG8/SMYLE
CC (PubMed:25217626). {ECO:0000269|PubMed:25217626,
CC ECO:0000269|PubMed:28814570}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10644998}.
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 mutually
CC exclusive complexes with APC and DCTN1. {ECO:0000269|PubMed:12388762}.
CC -!- PTM: Acetylation at Lys-220 by KAT2B/PCAF promotes dynamic kinetochore-
CC microtubule interactions in early mitosis.
CC {ECO:0000269|PubMed:23001180}.
CC -!- PTM: Crotonylated by KAT5 during mitosis, promoting astral microtubule
CC plasticity and dynamic connection between astral microtubules and the
CC cortex during mitotic chromosome segregation, thereby ensuring accurate
CC spindle positioning in mitosis (PubMed:34608293). Decrotonylated by
CC HDAC3 (PubMed:34608293). {ECO:0000269|PubMed:34608293}.
CC -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC 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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS13208.1; -.
DR PIR; I52726; I52726.
DR RefSeq; NP_036457.1; NM_012325.2.
DR RefSeq; XP_011526998.1; XM_011528696.2.
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=185-255.
DR PDB; 1YIG; X-ray; 2.00 A; A/B=185-255.
DR PDB; 2HKQ; X-ray; 1.86 A; A=191-268.
DR PDB; 2HL3; X-ray; 2.03 A; C=263-268.
DR PDB; 2HL5; X-ray; 1.93 A; A/B=191-268.
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; 3MTU; X-ray; 2.10 A; A/B/C/D=215-257.
DR PDB; 3MUD; X-ray; 2.20 A; C/D=226-257.
DR PDB; 3TQ7; X-ray; 2.30 A; A=191-268.
DR PDB; 4XA1; X-ray; 3.20 A; A/B/C/D=211-251.
DR PDB; 4XA3; X-ray; 2.55 A; A/B=215-251.
DR PDB; 4XA6; X-ray; 3.42 A; A/B/C/D=209-251.
DR PDB; 5JV3; X-ray; 2.01 A; A/B/C/D=210-257.
DR PDB; 5JVM; X-ray; 1.57 A; A/B=207-257.
DR PDB; 5JVP; X-ray; 2.10 A; A/B/C/D/E/F=210-257.
DR PDB; 5JVR; X-ray; 2.10 A; A/B/C/D/E/F/G/H=207-257.
DR PDB; 5JVS; X-ray; 2.25 A; A=207-257.
DR PDB; 5JVU; X-ray; 1.95 A; A/B=207-257.
DR PDB; 5JX1; X-ray; 1.67 A; A=210-257.
DR PDB; 5WLQ; X-ray; 3.10 A; A=208-257.
DR PDB; 6PF2; X-ray; 2.17 A; A/B=207-257.
DR PDB; 6PFP; X-ray; 2.20 A; A/B/C/D=207-257.
DR PDB; 6YF5; X-ray; 1.83 A; A/B/C/D=215-251.
DR PDB; 6YSH; X-ray; 2.83 A; A=215-251, B=215-250.
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; 3MTU; -.
DR PDBsum; 3MUD; -.
DR PDBsum; 3TQ7; -.
DR PDBsum; 4XA1; -.
DR PDBsum; 4XA3; -.
DR PDBsum; 4XA6; -.
DR PDBsum; 5JV3; -.
DR PDBsum; 5JVM; -.
DR PDBsum; 5JVP; -.
DR PDBsum; 5JVR; -.
DR PDBsum; 5JVS; -.
DR PDBsum; 5JVU; -.
DR PDBsum; 5JX1; -.
DR PDBsum; 5WLQ; -.
DR PDBsum; 6PF2; -.
DR PDBsum; 6PFP; -.
DR PDBsum; 6YF5; -.
DR PDBsum; 6YSH; -.
DR AlphaFoldDB; Q15691; -.
DR BMRB; Q15691; -.
DR SMR; Q15691; -.
DR BioGRID; 116581; 297.
DR DIP; DIP-38018N; -.
DR ELM; Q15691; -.
DR IntAct; Q15691; 147.
DR MINT; Q15691; -.
DR STRING; 9606.ENSP00000364721; -.
DR GlyGen; Q15691; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15691; -.
DR MetOSite; Q15691; -.
DR PhosphoSitePlus; Q15691; -.
DR SwissPalm; Q15691; -.
DR BioMuta; MAPRE1; -.
DR DMDM; 20138589; -.
DR OGP; Q15691; -.
DR REPRODUCTION-2DPAGE; IPI00017596; -.
DR EPD; Q15691; -.
DR jPOST; Q15691; -.
DR MassIVE; Q15691; -.
DR MaxQB; Q15691; -.
DR PaxDb; Q15691; -.
DR PeptideAtlas; Q15691; -.
DR PRIDE; Q15691; -.
DR ProteomicsDB; 60702; -.
DR Antibodypedia; 1211; 289 antibodies from 32 providers.
DR DNASU; 22919; -.
DR Ensembl; ENST00000375571.6; ENSP00000364721.5; ENSG00000101367.9.
DR GeneID; 22919; -.
DR KEGG; hsa:22919; -.
DR MANE-Select; ENST00000375571.6; ENSP00000364721.5; NM_012325.3; NP_036457.1.
DR UCSC; uc002wyh.3; human.
DR CTD; 22919; -.
DR DisGeNET; 22919; -.
DR GeneCards; MAPRE1; -.
DR HGNC; HGNC:6890; MAPRE1.
DR HPA; ENSG00000101367; Low tissue specificity.
DR MIM; 603108; gene.
DR neXtProt; NX_Q15691; -.
DR OpenTargets; ENSG00000101367; -.
DR PharmGKB; PA30634; -.
DR VEuPathDB; HostDB:ENSG00000101367; -.
DR eggNOG; KOG3000; Eukaryota.
DR GeneTree; ENSGT00490000043329; -.
DR HOGENOM; CLU_041744_1_1_1; -.
DR InParanoid; Q15691; -.
DR OMA; ICQEKES; -.
DR OrthoDB; 1237523at2759; -.
DR PhylomeDB; Q15691; -.
DR TreeFam; TF313620; -.
DR PathwayCommons; Q15691; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q15691; -.
DR SIGNOR; Q15691; -.
DR BioGRID-ORCS; 22919; 129 hits in 1085 CRISPR screens.
DR ChiTaRS; MAPRE1; human.
DR EvolutionaryTrace; Q15691; -.
DR GeneWiki; MAPRE1; -.
DR GenomeRNAi; 22919; -.
DR Pharos; Q15691; Tbio.
DR PRO; PR:Q15691; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q15691; protein.
DR Bgee; ENSG00000101367; Expressed in secondary oocyte and 209 other tissues.
DR Genevisible; Q15691; HS.
DR GO; GO:0031253; C:cell projection membrane; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0030981; C:cortical microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IDA:ARUK-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR GO; GO:1905721; C:mitotic spindle astral microtubule end; IDA:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IMP:ARUK-UCL.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IDA:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IEA:Ensembl.
DR GO; GO:0046785; P:microtubule polymerization; IEA:Ensembl.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:UniProtKB.
DR GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:1903033; P:positive regulation of microtubule plus-end binding; IEA:Ensembl.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; TAS:ARUK-UCL.
DR GO; GO:1902888; P:protein localization to astral microtubule; IDA:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IEA:Ensembl.
DR GO; GO:0035372; P:protein localization to microtubule; IDA:UniProtKB.
DR GO; GO:1904825; P:protein localization to microtubule plus-end; IBA:GO_Central.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR DisProt; DP01271; -.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR004953; EB1_C.
DR InterPro; IPR036133; EB1_C_sf.
DR InterPro; IPR027739; EB1_Meta.
DR InterPro; IPR027328; MAPRE.
DR PANTHER; PTHR10623; PTHR10623; 1.
DR PANTHER; PTHR10623:SF20; PTHR10623:SF20; 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; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Golgi apparatus; Microtubule;
KW Mitosis; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..268
FT /note="Microtubule-associated protein RP/EB family member
FT 1"
FT /id="PRO_0000213416"
FT DOMAIN 14..116
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 185..255
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 124..268
FT /note="Interaction with MTUS2/TIP150"
FT /evidence="ECO:0000269|PubMed:19543227"
FT REGION 146..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..268
FT /note="Interaction with CDK5RAP2"
FT /evidence="ECO:0000269|PubMed:19553473"
FT REGION 208..268
FT /note="DCTN1-binding"
FT /evidence="ECO:0000269|PubMed:14514668"
FT REGION 220..242
FT /note="APC-binding"
FT /evidence="ECO:0000269|PubMed:14514668"
FT COMPBIAS 150..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 66
FT /note="N6-crotonyllysine"
FT /evidence="ECO:0000269|PubMed:34608293"
FT MOD_RES 124
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:23001180"
FT MUTAGEN 59..60
FT /note="KK->EE: No effect."
FT /evidence="ECO:0000269|PubMed:12857735"
FT MUTAGEN 66
FT /note="K->R: Abolished crotonylation by KAT5."
FT /evidence="ECO:0000269|PubMed:34608293"
FT MUTAGEN 89
FT /note="K->E: Loss of binding to microtubules."
FT /evidence="ECO:0000269|PubMed:12857735"
FT MUTAGEN 220
FT /note="K->R: Abolished acetylation by KAT2B/PCAF, impairing
FT kinetochore-microtubule interactions during mitosis."
FT /evidence="ECO:0000269|PubMed:23001180"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:2QJZ"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:2QJZ"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:2QJZ"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2QJZ"
FT HELIX 68..85
FT /evidence="ECO:0007829|PDB:2QJZ"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:2QJZ"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:2R8U"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:2QJZ"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:2QJZ"
FT HELIX 192..230
FT /evidence="ECO:0007829|PDB:1WU9"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:1WU9"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:1WU9"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1WU9"
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
