MARE3_HUMAN
ID MARE3_HUMAN Reviewed; 281 AA.
AC Q9UPY8; B7WPK5; O00265; Q6FHB0; Q6FI15; Q9BZP7; Q9BZP8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Microtubule-associated protein RP/EB family member 3;
DE AltName: Full=EB1 protein family member 3;
DE Short=EBF3;
DE AltName: Full=End-binding protein 3;
DE Short=EB3;
DE AltName: Full=RP3;
GN Name=MAPRE3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH APC2, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Fetal brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RX PubMed=11161807; DOI=10.1006/geno.2000.6428;
RA Su L.-K., Qi Y.;
RT "Characterization of human MAPRE genes and their proteins.";
RL Genomics 71:142-149(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-200 (ISOFORM 1).
RX PubMed=9233623;
RA Renner C., Pfitzenmeier J.-P., Gerlach K., Held G., Ohnesorge S., Sahin U.,
RA Bauer S., Pfreundschuh M.;
RT "RP1, a new member of the adenomatous polyposis coli-binding EB1-like gene
RT family, is differentially expressed in activated T cells.";
RL J. Immunol. 159:1276-1283(1997).
RN [8]
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 [9]
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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP INTERACTION WITH SRCIN1.
RX PubMed=19146815; DOI=10.1016/j.neuron.2008.11.013;
RA Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S.,
RA Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J.,
RA Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.;
RT "Dynamic microtubules regulate dendritic spine morphology and synaptic
RT plasticity.";
RL Neuron 61:85-100(2009).
RN [13]
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 [14]
RP INTERACTION WITH SLAIN2 AND SLAIN1.
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP 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 [16]
RP INTERACTION WITH PDE4DIP.
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 [17]
RP FUNCTION, INTERACTION WITH AKAP9 AND PDE4DIP, AND MUTAGENESIS OF TYR-226
RP AND GLU-234.
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 [18]
RP STRUCTURE BY NMR OF 1-146.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CH domain of human microtubule-associated
RT protein RP/EB family member 3.";
RL Submitted (AUG-2005) to the PDB data bank.
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-130, FUNCTION, SUBUNIT,
RP INTERACTION WITH MAPRE1, AND SUBCELLULAR LOCATION.
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).
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. Promotes microtubule growth. May be involved in spindle
CC function by stabilizing microtubules and anchoring them at centrosomes.
CC Also acts as a regulator of minus-end microtubule organization:
CC interacts with the complex formed by AKAP9 and PDE4DIP, leading to
CC recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-
CC centrosomal minus-end microtubules to the Golgi, an important step for
CC polarized cell movement (PubMed:28814570). Promotes elongation of
CC CAMSAP2-decorated microtubule stretches on the minus-end of
CC microtubules (PubMed:28814570). May play a role in cell migration (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:19255245,
CC ECO:0000269|PubMed:28814570}.
CC -!- SUBUNIT: Interacts with APC2 (PubMed:10644998). Homodimer
CC (PubMed:19255245). Heterodimer with MAPRE1 (PubMed:19255245). Interacts
CC with DCTN1 and SRCIN1 (PubMed:14514668, PubMed:19146815). Binds to the
CC C-terminal domain of APC (PubMed:14514668). Binds monomeric and
CC polymerized tubulin (PubMed:10188731). Interacts (via C-terminus) with
CC CLIP1 (PubMed:17563362). Interacts with SLAIN2 and SLAIN1
CC (PubMed:21646404). Interacts with AKAP9 (PubMed:28814570). Interacts
CC with PDE4DIP (PubMed:28814570). Interacts with PDE4DIP isoform
CC 13/MMG8/SMYLE; this interaction is required for its recruitment to the
CC Golgi apparatus (PubMed:25217626). {ECO:0000269|PubMed:10188731,
CC ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:14514668,
CC ECO:0000269|PubMed:17563362, ECO:0000269|PubMed:19146815,
CC ECO:0000269|PubMed:19255245, ECO:0000269|PubMed:21646404,
CC ECO:0000269|PubMed:25217626, ECO:0000269|PubMed:28814570}.
CC -!- INTERACTION:
CC Q9UPY8; Q15327: ANKRD1; NbExp=5; IntAct=EBI-726739, EBI-5653378;
CC Q9UPY8; O95996: APC2; NbExp=7; IntAct=EBI-726739, EBI-1053045;
CC Q9UPY8; Q8NEU8: APPL2; NbExp=3; IntAct=EBI-726739, EBI-741261;
CC Q9UPY8; A1L168: C20orf202; NbExp=3; IntAct=EBI-726739, EBI-18396958;
CC Q9UPY8; Q96LM5: C4orf45; NbExp=3; IntAct=EBI-726739, EBI-12020542;
CC Q9UPY8; Q9C0I3-2: CCSER1; NbExp=3; IntAct=EBI-726739, EBI-17793327;
CC Q9UPY8; Q6WN34-2: CHRDL2; NbExp=3; IntAct=EBI-726739, EBI-12593838;
CC Q9UPY8; Q9NQ79: CRTAC1; NbExp=3; IntAct=EBI-726739, EBI-10205543;
CC Q9UPY8; Q13561: DCTN2; NbExp=3; IntAct=EBI-726739, EBI-715074;
CC Q9UPY8; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-726739, EBI-742054;
CC Q9UPY8; O60573: EIF4E2; NbExp=3; IntAct=EBI-726739, EBI-398610;
CC Q9UPY8; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-726739, EBI-7225287;
CC Q9UPY8; Q9NU39: FOXD4L1; NbExp=3; IntAct=EBI-726739, EBI-11320806;
CC Q9UPY8; Q8WXT5: FOXD4L4; NbExp=3; IntAct=EBI-726739, EBI-12911102;
CC Q9UPY8; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-726739, EBI-7960826;
CC Q9UPY8; P13984: GTF2F2; NbExp=3; IntAct=EBI-726739, EBI-1030560;
CC Q9UPY8; Q8N3J3-3: HROB; NbExp=3; IntAct=EBI-726739, EBI-11061081;
CC Q9UPY8; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-726739, EBI-11522367;
CC Q9UPY8; P05412: JUN; NbExp=3; IntAct=EBI-726739, EBI-852823;
CC Q9UPY8; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-726739, EBI-9478422;
CC Q9UPY8; Q9Y448: KNSTRN; NbExp=3; IntAct=EBI-726739, EBI-373334;
CC Q9UPY8; P28838: LAP3; NbExp=3; IntAct=EBI-726739, EBI-2339312;
CC Q9UPY8; Q969G2: LHX4; NbExp=3; IntAct=EBI-726739, EBI-2865388;
CC Q9UPY8; P25791: LMO2; NbExp=5; IntAct=EBI-726739, EBI-739696;
CC Q9UPY8; P25791-3: LMO2; NbExp=6; IntAct=EBI-726739, EBI-11959475;
CC Q9UPY8; Q15691: MAPRE1; NbExp=19; IntAct=EBI-726739, EBI-1004115;
CC Q9UPY8; Q15555: MAPRE2; NbExp=7; IntAct=EBI-726739, EBI-739717;
CC Q9UPY8; Q9UPY8: MAPRE3; NbExp=7; IntAct=EBI-726739, EBI-726739;
CC Q9UPY8; P10636: MAPT; NbExp=3; IntAct=EBI-726739, EBI-366182;
CC Q9UPY8; Q9H992: MARCHF7; NbExp=5; IntAct=EBI-726739, EBI-949983;
CC Q9UPY8; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-726739, EBI-16439278;
CC Q9UPY8; P52815: MRPL12; NbExp=3; IntAct=EBI-726739, EBI-358272;
CC Q9UPY8; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-726739, EBI-9640281;
CC Q9UPY8; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-726739, EBI-79165;
CC Q9UPY8; Q01851: POU4F1; NbExp=3; IntAct=EBI-726739, EBI-17480471;
CC Q9UPY8; P25786: PSMA1; NbExp=4; IntAct=EBI-726739, EBI-359352;
CC Q9UPY8; P20618: PSMB1; NbExp=3; IntAct=EBI-726739, EBI-372273;
CC Q9UPY8; Q6PGN9: PSRC1; NbExp=3; IntAct=EBI-726739, EBI-7392664;
CC Q9UPY8; Q04864-2: REL; NbExp=3; IntAct=EBI-726739, EBI-10829018;
CC Q9UPY8; O00560: SDCBP; NbExp=6; IntAct=EBI-726739, EBI-727004;
CC Q9UPY8; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-726739, EBI-11522811;
CC Q9UPY8; P0CI01: SPDYE6; NbExp=3; IntAct=EBI-726739, EBI-11960469;
CC Q9UPY8; Q9UL54: TAOK2; NbExp=3; IntAct=EBI-726739, EBI-352832;
CC Q9UPY8; Q6ZNM6: TEX43; NbExp=3; IntAct=EBI-726739, EBI-18115728;
CC Q9UPY8; Q08117-2: TLE5; NbExp=3; IntAct=EBI-726739, EBI-11741437;
CC Q9UPY8; Q9BWF2: TRAIP; NbExp=3; IntAct=EBI-726739, EBI-1756205;
CC Q9UPY8; Q14142: TRIM14; NbExp=3; IntAct=EBI-726739, EBI-2820256;
CC Q9UPY8; Q12815: TROAP; NbExp=7; IntAct=EBI-726739, EBI-2349743;
CC Q9UPY8; Q99757: TXN2; NbExp=6; IntAct=EBI-726739, EBI-2932492;
CC Q9UPY8; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-726739, EBI-12111538;
CC Q9UPY8; Q96GY0: ZC2HC1A; NbExp=3; IntAct=EBI-726739, EBI-5458880;
CC Q9UPY8; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-726739, EBI-14104088;
CC Q9UPY8; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-726739, EBI-11035148;
CC Q9UPY8; Q8IVP9: ZNF547; NbExp=3; IntAct=EBI-726739, EBI-12895421;
CC Q9UPY8; P14873: Map1b; Xeno; NbExp=4; IntAct=EBI-726739, EBI-764653;
CC Q9UPY8; Q9QWI6-2: Srcin1; Xeno; NbExp=5; IntAct=EBI-726739, EBI-775607;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:19255245,
CC ECO:0000269|PubMed:28814570}. Note=Associated with the microtubule
CC network. Detected at the plus end of microtubules.
CC {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:19255245,
CC ECO:0000269|PubMed:28814570}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=EBF3-L;
CC IsoId=Q9UPY8-1; Sequence=Displayed;
CC Name=2; Synonyms=EBF3-S;
CC IsoId=Q9UPY8-2; Sequence=VSP_012947;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain and muscle.
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:14514668}.
CC -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK07556.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK07557.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA72060.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB025186; BAA82958.1; -; mRNA.
DR EMBL; AF288787; AAK07556.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF288787; AAK07557.1; ALT_INIT; Genomic_DNA.
DR EMBL; CR536523; CAG38760.1; -; mRNA.
DR EMBL; CR541845; CAG46643.1; -; mRNA.
DR EMBL; AC013472; AAY14653.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00660.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00662.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00663.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00666.1; -; Genomic_DNA.
DR EMBL; BC011557; AAH11557.1; -; mRNA.
DR EMBL; Y11174; CAA72060.1; ALT_FRAME; mRNA.
DR CCDS; CCDS1731.1; -. [Q9UPY8-1]
DR RefSeq; NP_001289979.1; NM_001303050.1. [Q9UPY8-1]
DR RefSeq; NP_036458.2; NM_012326.3. [Q9UPY8-1]
DR RefSeq; XP_006712030.1; XM_006711967.3. [Q9UPY8-2]
DR RefSeq; XP_011531002.1; XM_011532700.1. [Q9UPY8-2]
DR RefSeq; XP_016859086.1; XM_017003597.1. [Q9UPY8-2]
DR PDB; 1WYO; NMR; -; A=1-146.
DR PDB; 3CO1; X-ray; 1.40 A; A=1-130.
DR PDB; 3JAK; EM; 3.50 A; M/N=1-200.
DR PDB; 3JAL; EM; 3.50 A; M/N=1-200.
DR PDB; 3JAR; EM; 3.50 A; M/N=1-200.
DR PDB; 3TQ7; X-ray; 2.30 A; B=200-281.
DR PDB; 7SJ9; EM; 3.80 A; M/N=1-281.
DR PDBsum; 1WYO; -.
DR PDBsum; 3CO1; -.
DR PDBsum; 3JAK; -.
DR PDBsum; 3JAL; -.
DR PDBsum; 3JAR; -.
DR PDBsum; 3TQ7; -.
DR PDBsum; 7SJ9; -.
DR AlphaFoldDB; Q9UPY8; -.
DR BMRB; Q9UPY8; -.
DR SMR; Q9UPY8; -.
DR BioGRID; 116584; 226.
DR DIP; DIP-56069N; -.
DR IntAct; Q9UPY8; 69.
DR MINT; Q9UPY8; -.
DR STRING; 9606.ENSP00000233121; -.
DR iPTMnet; Q9UPY8; -.
DR PhosphoSitePlus; Q9UPY8; -.
DR BioMuta; MAPRE3; -.
DR DMDM; 20138791; -.
DR EPD; Q9UPY8; -.
DR jPOST; Q9UPY8; -.
DR MassIVE; Q9UPY8; -.
DR MaxQB; Q9UPY8; -.
DR PaxDb; Q9UPY8; -.
DR PeptideAtlas; Q9UPY8; -.
DR PRIDE; Q9UPY8; -.
DR ProteomicsDB; 85475; -. [Q9UPY8-1]
DR ProteomicsDB; 85476; -. [Q9UPY8-2]
DR Antibodypedia; 1949; 264 antibodies from 38 providers.
DR DNASU; 22924; -.
DR Ensembl; ENST00000233121.7; ENSP00000233121.2; ENSG00000084764.12. [Q9UPY8-1]
DR Ensembl; ENST00000402218.1; ENSP00000385715.1; ENSG00000084764.12. [Q9UPY8-2]
DR Ensembl; ENST00000405074.7; ENSP00000383915.3; ENSG00000084764.12. [Q9UPY8-2]
DR Ensembl; ENST00000648289.1; ENSP00000497057.1; ENSG00000084764.12. [Q9UPY8-2]
DR GeneID; 22924; -.
DR KEGG; hsa:22924; -.
DR MANE-Select; ENST00000233121.7; ENSP00000233121.2; NM_012326.4; NP_036458.2.
DR UCSC; uc002rhw.4; human. [Q9UPY8-1]
DR CTD; 22924; -.
DR DisGeNET; 22924; -.
DR GeneCards; MAPRE3; -.
DR HGNC; HGNC:6892; MAPRE3.
DR HPA; ENSG00000084764; Tissue enhanced (skeletal).
DR MIM; 605788; gene.
DR neXtProt; NX_Q9UPY8; -.
DR OpenTargets; ENSG00000084764; -.
DR PharmGKB; PA30636; -.
DR VEuPathDB; HostDB:ENSG00000084764; -.
DR eggNOG; KOG3000; Eukaryota.
DR GeneTree; ENSGT00490000043329; -.
DR HOGENOM; CLU_041744_1_0_1; -.
DR InParanoid; Q9UPY8; -.
DR OMA; VQHAKEM; -.
DR OrthoDB; 1237523at2759; -.
DR PhylomeDB; Q9UPY8; -.
DR TreeFam; TF313620; -.
DR PathwayCommons; Q9UPY8; -.
DR SignaLink; Q9UPY8; -.
DR SIGNOR; Q9UPY8; -.
DR BioGRID-ORCS; 22924; 7 hits in 1079 CRISPR screens.
DR ChiTaRS; MAPRE3; human.
DR EvolutionaryTrace; Q9UPY8; -.
DR GeneWiki; MAPRE3; -.
DR GenomeRNAi; 22924; -.
DR Pharos; Q9UPY8; Tbio.
DR PRO; PR:Q9UPY8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UPY8; protein.
DR Bgee; ENSG00000084764; Expressed in Brodmann (1909) area 10 and 198 other tissues.
DR ExpressionAtlas; Q9UPY8; baseline and differential.
DR Genevisible; Q9UPY8; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL.
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:0030496; C:midbody; ISS:BHF-UCL.
DR GO; GO:1905721; C:mitotic spindle astral microtubule end; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; ISS:BHF-UCL.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:ARUK-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:BHF-UCL.
DR GO; GO:1903033; P:positive regulation of microtubule plus-end binding; IEA:Ensembl.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:ARUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:0008104; P:protein localization; TAS:ARUK-UCL.
DR GO; GO:1904825; P:protein localization to microtubule plus-end; IBA:GO_Central.
DR GO; GO:0031113; P:regulation of microtubule polymerization; IMP:ARUK-UCL.
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 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; IPR027738; EB3.
DR InterPro; IPR027328; MAPRE.
DR PANTHER; PTHR10623; PTHR10623; 1.
DR PANTHER; PTHR10623:SF10; PTHR10623:SF10; 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; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..281
FT /note="Microtubule-associated protein RP/EB family member
FT 3"
FT /id="PRO_0000213428"
FT DOMAIN 14..116
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 194..264
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 157..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..281
FT /note="DCTN1-binding"
FT REGION 217..260
FT /note="APC-binding"
FT REGION 261..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..281
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PER3"
FT VAR_SEQ 142..156
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11161807"
FT /id="VSP_012947"
FT MUTAGEN 226
FT /note="Y->A: Loss of localization of CAMSAP2 stretches to
FT the Golgi apparatus; when associated with A-234."
FT /evidence="ECO:0000269|PubMed:28814570"
FT MUTAGEN 234
FT /note="E->A: Loss of localization of CAMSAP2 stretches to
FT the Golgi apparatus; when associated with A-226."
FT /evidence="ECO:0000269|PubMed:28814570"
FT CONFLICT 2
FT /note="A -> P (in Ref. 7; CAA72060)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="E -> V (in Ref. 7; CAA72060)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="D -> G (in Ref. 7; CAA72060)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="C -> S (in Ref. 3; CAG38760)"
FT /evidence="ECO:0000305"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:3CO1"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:3CO1"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:3CO1"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3JAL"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3CO1"
FT HELIX 68..85
FT /evidence="ECO:0007829|PDB:3CO1"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:3CO1"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:3CO1"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:3CO1"
FT HELIX 206..238
FT /evidence="ECO:0007829|PDB:3TQ7"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:3TQ7"
SQ SEQUENCE 281 AA; 31982 MW; 0DA45E89A0B993D3 CRC64;
MAVNVYSTSV TSENLSRHDM LAWVNDSLHL NYTKIEQLCS GAAYCQFMDM LFPGCVHLRK
VKFQAKLEHE YIHNFKVLQA AFKKMGVDKI IPVEKLVKGK FQDNFEFIQW FKKFFDANYD
GKDYNPLLAR QGQDVAPPPN PGDQIFNKSK KLIGTAVPQR TSPTGPKNMQ TSGRLSNVAP
PCILRKNPPS ARNGGHETDA QILELNQQLV DLKLTVDGLE KERDFYFSKL RDIELICQEH
ESENSPVISG IIGILYATEE GFAPPEDDEI EEHQQEDQDE Y
