CLAP2_HUMAN
ID CLAP2_HUMAN Reviewed; 1294 AA.
AC O75122; B2RTR1; F5H604; Q7L8F6; Q8N6R6; Q9BQT3; Q9BQT4; Q9H7A3; Q9NSZ2;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=CLIP-associating protein 2;
DE AltName: Full=Cytoplasmic linker-associated protein 2;
DE AltName: Full=Protein Orbit homolog 2;
DE Short=hOrbit2;
GN Name=CLASP2; Synonyms=KIAA0627;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-9 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 1-15 (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH CLIP2; MICROTUBULES AND RSN.
RC TISSUE=Brain;
RX PubMed=11290329; DOI=10.1016/s0092-8674(01)00288-4;
RA Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
RA Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
RA Galjart N.;
RT "Clasps are CLIP-115 and -170 associating proteins involved in the regional
RT regulation of microtubule dynamics in motile fibroblasts.";
RL Cell 104:923-935(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 939-1294 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1128-1294 (ISOFORM 1).
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15207236; DOI=10.1016/j.neuron.2004.05.020;
RA Lee H., Engel U., Rusch J., Scherrer S., Sheard K., Van Vactor D.;
RT "The microtubule plus end tracking protein Orbit/MAST/CLASP acts downstream
RT of the tyrosine kinase Abl in mediating axon guidance.";
RL Neuron 42:913-926(2004).
RN [8]
RP FUNCTION, INTERACTION WITH MAPRE1; MAPRE3; MICROTUBULES AND RSN, AND
RP SUBCELLULAR LOCATION.
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 [9]
RP INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY
RP GSK3B.
RX PubMed=15955847; DOI=10.1083/jcb.200412114;
RA Wittmann T., Waterman-Storer C.M.;
RT "Spatial regulation of CLASP affinity for microtubules by Rac1 and GSK3beta
RT in migrating epithelial cells.";
RL J. Cell Biol. 169:929-939(2005).
RN [10]
RP ERRATUM OF PUBMED:15955847.
RA Wittmann T., Waterman-Storer C.M.;
RL J. Cell Biol. 171:393-393(2005).
RN [11]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERC1;
RP PHLDB2 AND RSN, AND SUBCELLULAR LOCATION.
RX PubMed=16824950; DOI=10.1016/j.devcel.2006.05.012;
RA Lansbergen G., Grigoriev I., Mimori-Kiyosue Y., Ohtsuka T., Higa S.,
RA Kitajima I., Demmers J., Galjart N., Houtsmuller A.B., Grosveld F.,
RA Akhmanova A.;
RT "CLASPs attach microtubule plus ends to the cell cortex through a complex
RT with LL5beta.";
RL Dev. Cell 11:21-32(2006).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16866869; DOI=10.1111/j.1365-2443.2006.00990.x;
RA Mimori-Kiyosue Y., Grigoriev I., Sasaki H., Matsui C., Akhmanova A.,
RA Tsukita S., Vorobjev I.;
RT "Mammalian CLASPs are required for mitotic spindle organization and
RT kinetochore alignment.";
RL Genes Cells 11:845-857(2006).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16914514; DOI=10.1091/mbc.e06-07-0579;
RA Pereira A.L., Pereira A.J., Maia A.R.R., Drabek K., Sayas C.L.,
RA Hergert P.J., Lince-Faria M., Matos I., Duque C., Stepanova T.,
RA Rieder C.L., Earnshaw W.C., Galjart N., Maiato H.;
RT "Mammalian CLASP1 and CLASP2 cooperate to ensure mitotic fidelity by
RT regulating spindle and kinetochore function.";
RL Mol. Biol. Cell 17:4526-4542(2006).
RN [14]
RP FUNCTION, INTERACTION WITH GCC2, AND SUBCELLULAR LOCATION.
RX PubMed=17543864; DOI=10.1016/j.devcel.2007.04.002;
RA Efimov A., Kharitonov A., Efimova N., Loncarek J., Miller P.M.,
RA Andreyeva N., Gleeson P., Galjart N., Maia A.R., McLeod I.X.,
RA Yates J.R. III, Maiato H., Khodjakov A., Akhmanova A., Kaverina I.;
RT "Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at
RT the trans-Golgi network.";
RL Dev. Cell 12:917-930(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-525; SER-529;
RP SER-596 AND SER-1029, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 MAPRE1, SUBCELLULAR LOCATION, DOMAIN MICROTUBULE TIP
RP LOCALIZATION SIGNAL, AND MUTAGENESIS OF 496-ILE-PRO-497 AND
RP 519-ILE-PRO-520.
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).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-596 AND SER-1029,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20937854; DOI=10.1073/pnas.1000975107;
RA Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.;
RT "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the
RT plasma membrane of migrating cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-370; SER-455 AND
RP SER-596, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-330; SER-360;
RP SER-370; SER-459; SER-463; SER-478; SER-489; SER-507; SER-525; SER-529;
RP SER-585; SER-587; SER-596; SER-621; THR-787; SER-892; SER-952; SER-955;
RP SER-1013 AND SER-1029, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION BY
RP 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 [27]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 60-310, FUNCTION, SUBUNIT,
RP INTERACTION WITH MAPRE1, DOMAIN, AND MUTAGENESIS OF TRP-106; LYS-191;
RP 496-ILE-PRO-497; SER-499; SER-507; 519-ILE-PRO-520; SER-525; SER-529;
RP SER-533; SER-537; SER-541; TRP-667; LYS-833; ARG-838 AND LYS-839.
RX PubMed=26003921; DOI=10.1016/j.jmb.2015.05.012;
RA Maki T., Grimaldi A.D., Fuchigami S., Kaverina I., Hayashi I.;
RT "CLASP2 has two distinct TOG domains that contribute differently to
RT microtubule dynamics.";
RL J. Mol. Biol. 427:2379-2395(2015).
CC -!- FUNCTION: Microtubule plus-end tracking protein that promotes the
CC stabilization of dynamic microtubules (PubMed:26003921). Involved in
CC the nucleation of noncentrosomal microtubules originating from the
CC trans-Golgi network (TGN). Required for the polarization of the
CC cytoplasmic microtubule arrays in migrating cells towards the leading
CC edge of the cell. May act at the cell cortex to enhance the frequency
CC of rescue of depolymerizing microtubules by attaching their plus-ends
CC to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950).
CC This cortical microtubule stabilizing activity is regulated at least in
CC part by phosphatidylinositol 3-kinase signaling. Also performs a
CC similar stabilizing function at the kinetochore which is essential for
CC the bipolar alignment of chromosomes on the mitotic spindle
CC (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-
CC dependent stabilization of microtubules at the cell cortex.
CC {ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:15631994,
CC ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:16866869,
CC ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:17543864,
CC ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:26003921}.
CC -!- SUBUNIT: Interacts with microtubules (PubMed:11290329, PubMed:15631994,
CC PubMed:15955847, PubMed:26003921). Interacts with MAPRE1; probably
CC required for targeting to the growing microtubule plus ends
CC (PubMed:15631994, PubMed:19632184, PubMed:26003921). Interacts with
CC CLIP2, ERC1, MAPRE3, PHLDB2 and RSN (PubMed:11290329, PubMed:15631994).
CC The interaction with ERC1 may be mediated by PHLDB2 (PubMed:16824950).
CC Interacts with GCC2; recruits CLASP2 to Golgi membranes
CC (PubMed:17543864). Interacts with MACF1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BRT1, ECO:0000269|PubMed:11290329,
CC ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:15955847,
CC ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:17543864,
CC ECO:0000269|PubMed:19632184}.
CC -!- INTERACTION:
CC O75122; Q15691: MAPRE1; NbExp=3; IntAct=EBI-913524, EBI-1004115;
CC O75122; O55156: Clip2; Xeno; NbExp=3; IntAct=EBI-913524, EBI-349416;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:20937854}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:16914514}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:16866869,
CC ECO:0000269|PubMed:16914514}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q8BRT1}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:17543864}. Cell membrane
CC {ECO:0000269|PubMed:20937854}. Cell projection, ruffle membrane
CC {ECO:0000269|PubMed:20937854}. Note=Localizes to microtubule plus ends
CC (PubMed:15631994). Localizes to centrosomes, kinetochores and the
CC mitotic spindle from prometaphase. Subsequently localizes to the
CC spindle midzone from anaphase and to the midbody from telophase
CC (PubMed:16866869, PubMed:16914514). In migrating cells localizes to the
CC plus ends of microtubules within the cell body and to the entire
CC microtubule lattice within the lamella. Localizes to the cell cortex
CC and this requires ERC1 and PHLDB2 (PubMed:16824950). The MEMO1-RHOA-
CC DIAPH1 signaling pathway controls localization of the phosphorylated
CC form to the cell membrane. {ECO:0000269|PubMed:15631994,
CC ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:16866869,
CC ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:20937854}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms exist.;
CC Name=1; Synonyms=CLASP2 gamma;
CC IsoId=O75122-1; Sequence=Displayed;
CC Name=2; Synonyms=CLASP2 beta;
CC IsoId=O75122-2; Sequence=VSP_015805, VSP_015806, VSP_015807;
CC Name=3;
CC IsoId=O75122-3; Sequence=VSP_057273, VSP_057274, VSP_057275,
CC VSP_057276;
CC -!- TISSUE SPECIFICITY: Brain-specific.
CC -!- DOMAIN: The two SXIP sequence motifs mediate interaction with MAPRE1;
CC this is necessary for targeting to growing microtubule plus ends.
CC {ECO:0000269|PubMed:19632184}.
CC -!- DOMAIN: Two TOG regions display structural characteristics similar to
CC HEAT repeat domains and mediate interaction with microtubules.
CC {ECO:0000269|PubMed:26003921}.
CC -!- PTM: Phosphorylated by GSK3B. Phosphorylation reduces MAPRE1 binding
CC (PubMed:26003921). Phosphorylation by GSK3B may negatively regulate
CC binding to microtubule lattices in lamella.
CC {ECO:0000269|PubMed:15955847, ECO:0000305|PubMed:26003921}.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31602.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14995.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014527; BAA31602.2; ALT_INIT; mRNA.
DR EMBL; AC093114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029035; AAH29035.1; -; mRNA.
DR EMBL; BC140778; AAI40779.1; -; mRNA.
DR EMBL; AJ288058; CAC35157.1; -; mRNA.
DR EMBL; AJ288059; CAC35158.1; -; mRNA.
DR EMBL; AL137636; CAB70852.1; -; mRNA.
DR EMBL; AK024770; BAB14995.1; ALT_INIT; mRNA.
DR PIR; T00386; T00386.
DR RefSeq; NP_001193973.1; NM_001207044.1. [O75122-1]
DR RefSeq; NP_055912.2; NM_015097.2. [O75122-3]
DR PDB; 3WOY; X-ray; 2.10 A; A=60-310.
DR PDB; 5NR4; X-ray; 1.20 A; A/B=1111-1275.
DR PDBsum; 3WOY; -.
DR PDBsum; 5NR4; -.
DR AlphaFoldDB; O75122; -.
DR SMR; O75122; -.
DR BioGRID; 116743; 101.
DR DIP; DIP-36804N; -.
DR IntAct; O75122; 42.
DR MINT; O75122; -.
DR STRING; 9606.ENSP00000417518; -.
DR GlyGen; O75122; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O75122; -.
DR MetOSite; O75122; -.
DR PhosphoSitePlus; O75122; -.
DR BioMuta; CLASP2; -.
DR EPD; O75122; -.
DR jPOST; O75122; -.
DR MassIVE; O75122; -.
DR MaxQB; O75122; -.
DR PaxDb; O75122; -.
DR PeptideAtlas; O75122; -.
DR PRIDE; O75122; -.
DR ProteomicsDB; 27038; -.
DR ProteomicsDB; 49777; -. [O75122-1]
DR ProteomicsDB; 49778; -. [O75122-2]
DR Antibodypedia; 27973; 362 antibodies from 32 providers.
DR DNASU; 23122; -.
DR Ensembl; ENST00000313350.10; ENSP00000324364.6; ENSG00000163539.18. [O75122-2]
DR Ensembl; ENST00000359576.9; ENSP00000352581.6; ENSG00000163539.18. [O75122-3]
DR Ensembl; ENST00000480013.6; ENSP00000417518.2; ENSG00000163539.18. [O75122-1]
DR GeneID; 23122; -.
DR KEGG; hsa:23122; -.
DR UCSC; uc003cfv.4; human. [O75122-1]
DR CTD; 23122; -.
DR DisGeNET; 23122; -.
DR GeneCards; CLASP2; -.
DR HGNC; HGNC:17078; CLASP2.
DR HPA; ENSG00000163539; Tissue enhanced (brain, retina).
DR MIM; 605853; gene.
DR neXtProt; NX_O75122; -.
DR OpenTargets; ENSG00000163539; -.
DR PharmGKB; PA38435; -.
DR VEuPathDB; HostDB:ENSG00000163539; -.
DR eggNOG; KOG2956; Eukaryota.
DR GeneTree; ENSGT00940000155574; -.
DR HOGENOM; CLU_014496_2_0_1; -.
DR InParanoid; O75122; -.
DR OrthoDB; 66632at2759; -.
DR PhylomeDB; O75122; -.
DR PathwayCommons; O75122; -.
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-428890; Role of ABL in ROBO-SLIT signaling.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; O75122; -.
DR SIGNOR; O75122; -.
DR BioGRID-ORCS; 23122; 20 hits in 319 CRISPR screens.
DR ChiTaRS; CLASP2; human.
DR GeneWiki; CLASP2; -.
DR GenomeRNAi; 23122; -.
DR Pharos; O75122; Tbio.
DR PRO; PR:O75122; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O75122; protein.
DR Bgee; ENSG00000163539; Expressed in corpus callosum and 203 other tissues.
DR ExpressionAtlas; O75122; baseline and differential.
DR Genevisible; O75122; HS.
DR GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
DR GO; GO:0045180; C:basal cortex; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:1903754; C:cortical microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005828; C:kinetochore microtubule; TAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0002162; F:dystroglycan binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:UniProtKB.
DR GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0034453; P:microtubule anchoring; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; IMP:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; NAS:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:UniProtKB.
DR GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; IMP:UniProtKB.
DR GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; IDA:UniProtKB.
DR GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; IMP:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0030516; P:regulation of axon extension; IDA:UniProtKB.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0010470; P:regulation of gastrulation; IMP:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; IDA:UniProtKB.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IMP:UniProtKB.
DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
DR GO; GO:0006903; P:vesicle targeting; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR034085; TOG.
DR Pfam; PF12348; CLASP_N; 1.
DR SMART; SM01349; TOG; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division;
KW Cell membrane; Cell projection; Centromere; Chromosome; Cytoplasm;
KW Cytoskeleton; Golgi apparatus; Kinetochore; Membrane; Microtubule; Mitosis;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1294
FT /note="CLIP-associating protein 2"
FT /id="PRO_0000089849"
FT REPEAT 173..208
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 209..245
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 250..287
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 710..747
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 772..809
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 1054..1091
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 1098..1135
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 1216..1253
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..311
FT /note="TOG 1"
FT /evidence="ECO:0000269|PubMed:26003921"
FT REGION 314..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..580
FT /note="Interaction with microtubules, MAPRE1 and MAPRE3"
FT /evidence="ECO:0000269|PubMed:15631994"
FT REGION 488..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..881
FT /note="TOG 2"
FT /evidence="ECO:0000269|PubMed:26003921"
FT REGION 872..1294
FT /note="Interaction with RSN and localization to the Golgi
FT and kinetochores"
FT REGION 878..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1294
FT /note="Required for cortical localization"
FT MOTIF 494..497
FT /note="SXIP motif 1; mediates interaction with MAPRE1 and
FT targeting to microtubule plus ends"
FT /evidence="ECO:0000269|PubMed:19632184,
FT ECO:0000269|PubMed:26003921"
FT MOTIF 517..520
FT /note="SXIP motif 2; mediates interaction with MAPRE1 and
FT targeting to microtubule plus ends"
FT /evidence="ECO:0000269|PubMed:19632184,
FT ECO:0000269|PubMed:26003921"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JD4"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BRT1"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JD4"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BRT1"
FT MOD_RES 787
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 952
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 955
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..6
FT /note="MAMGDD -> MRRLICKRICDY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11290329,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015805"
FT VAR_SEQ 1..5
FT /note="MAMGD -> MEPRSMEYFCAQVQQKDVGGRLQVGQELLLYLGAPGAISDLEE
FT DLGRLGKTVDALTGWVGSSNYRVSLMGLEILSAFVDRLSTRFKSYVAMVIVALIDRMGD
FT AKDKVRDEAQTLILKLMDQVAPPMYIWEQLASGFKHKNFRSREGVCLCLIETLNIFGAQ
FT PLVISKLIPHLCILFGDSNSQVRDAAILAIVEIYRHVGEKVRMDLYKRGIPPARLEMIF
FT AKFDEVQSSGGMILSVCK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057273"
FT VAR_SEQ 54
FT /note="G -> GA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057274"
FT VAR_SEQ 410..425
FT /note="DTSDKLDGTASEDGRV -> CEAFWRSGRTAKLYSV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11290329,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015806"
FT VAR_SEQ 426..1294
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11290329,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015807"
FT VAR_SEQ 550..570
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057275"
FT VAR_SEQ 606
FT /note="L -> LLLGDIRTK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057276"
FT MUTAGEN 106
FT /note="W->E: Decreases affinity for microtubules; when
FT associated with A-191; E-667; E-833; A-838 and A-839."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 191
FT /note="K->A: Decreases affinity for microtubules; when
FT associated with E-106; E-667; E-833; A-838 and A-839."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 496..497
FT /note="IP->AA: No effect on MAPRE1 binding. Abolishes
FT interaction with MAPRE1; when associated with 519-A-A-520."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 496..497
FT /note="IP->SS: Reduced targeting to the growing microtubule
FT plus ends. Loss of interaction with MAPRE1 and targeting to
FT the growing microtubule plus ends; when associated with
FT 519-S-S-520."
FT /evidence="ECO:0000269|PubMed:19632184"
FT MUTAGEN 499
FT /note="S->D: Phosphomimetic mutant that reduces MAPRE1
FT binding; when associated with D-503; D-507; D-525; D-529;
FT D-533; D-537 and D-541."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 503
FT /note="S->D: Phosphomimetic mutant that reduces MAPRE1
FT binding; when associated with D-499; D-507; D-525; D-529;
FT D-533; D-537 and D-541."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 507
FT /note="S->D: Phosphomimetic mutant that reduces MAPRE1
FT binding; when associated with D-499; D-503; D-525; D-529;
FT D-533; D-537 and D-541."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 519..520
FT /note="IP->AA: No effect on MAPRE1 binding. Abolishes
FT interaction with MAPRE1; when associated with 496-A-A-497."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 519..520
FT /note="IP->SS: Reduced targeting to the growing microtubule
FT plus ends. Loss of interaction with MAPRE1 and targeting to
FT the growing microtubule plus ends; when associated with
FT 496-S-S-497."
FT /evidence="ECO:0000269|PubMed:19632184"
FT MUTAGEN 525
FT /note="S->D: Phosphomimetic mutant that reduces MAPRE1
FT binding; when associated with D-499; D-503; D-507; D-529;
FT D-533; D-537 and D-541."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 529
FT /note="S->D: Phosphomimetic mutant that reduces MAPRE1
FT binding; when associated with D-499; D-503; D-507; D-525;
FT D-533; D-537 and D-541."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 533
FT /note="S->D: Phosphomimetic mutant that reduces MAPRE1
FT binding; when associated with D-499; D-503; D-507; D-525;
FT D-529; D-537 and D-541."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 537
FT /note="S->D: Phosphomimetic mutant that reduces MAPRE1
FT binding; when associated with D-499; D-503; D-507; D-525;
FT D-529; D-533 and D-541."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 541
FT /note="S->D: Phosphomimetic mutant that reduces MAPRE1
FT binding; when associated with D-499; D-503; D-507; D-525;
FT D-529; D-533 and D-537."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 667
FT /note="W->E: Decreases affinity for microtubules; when
FT associated with E-106; A-191; E-833; A-838 and A-839."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 833
FT /note="K->E: Decreases affinity for microtubules; when
FT associated with E-106; A-191; E-667; A-838 and A-839."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 838
FT /note="R->A: Decreases affinity for microtubules; when
FT associated with E-106; A-191; E-667; E-833 and A-839."
FT /evidence="ECO:0000269|PubMed:26003921"
FT MUTAGEN 839
FT /note="K->A: Decreases affinity for microtubules; when
FT associated with E-106; A-191; E-667; E-833 and A-838."
FT /evidence="ECO:0000269|PubMed:26003921"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 85..100
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 150..167
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 191..207
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 226..242
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 252..263
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 268..284
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:3WOY"
FT HELIX 1116..1133
FT /evidence="ECO:0007829|PDB:5NR4"
FT HELIX 1134..1140
FT /evidence="ECO:0007829|PDB:5NR4"
FT HELIX 1141..1151
FT /evidence="ECO:0007829|PDB:5NR4"
FT HELIX 1157..1173
FT /evidence="ECO:0007829|PDB:5NR4"
FT HELIX 1177..1183
FT /evidence="ECO:0007829|PDB:5NR4"
FT HELIX 1184..1188
FT /evidence="ECO:0007829|PDB:5NR4"
FT HELIX 1192..1209
FT /evidence="ECO:0007829|PDB:5NR4"
FT HELIX 1218..1228
FT /evidence="ECO:0007829|PDB:5NR4"
FT HELIX 1234..1251
FT /evidence="ECO:0007829|PDB:5NR4"
FT HELIX 1254..1259
FT /evidence="ECO:0007829|PDB:5NR4"
FT HELIX 1266..1275
FT /evidence="ECO:0007829|PDB:5NR4"
SQ SEQUENCE 1294 AA; 141064 MW; EAD31F728BC63B4B CRC64;
MAMGDDKSFD DEESVDGNRP SSAASAFKVP APKTSGNPAN SARKPGSAGG PKVGGASKEG
GAGAVDEDDF IKAFTDVPSI QIYSSRELEE TLNKIREILS DDKHDWDQRA NALKKIRSLL
VAGAAQYDCF FQHLRLLDGA LKLSAKDLRS QVVREACITV AHLSTVLGNK FDHGAEAIVP
TLFNLVPNSA KVMATSGCAA IRFIIRHTHV PRLIPLITSN CTSKSVPVRR RSFEFLDLLL
QEWQTHSLER HAAVLVETIK KGIHDADAEA RVEARKTYMG LRNHFPGEAE TLYNSLEPSY
QKSLQTYLKS SGSVASLPQS DRSSSSSQES LNRPFSSKWS TANPSTVAGR VSAGSSKASS
LPGSLQRSRS DIDVNAAAGA KAHHAAGQSV RSGRLGAGAL NAGSYASLED TSDKLDGTAS
EDGRVRAKLS APLAGMGNAK ADSRGRSRTK MVSQSQPGSR SGSPGRVLTT TALSTVSSGV
QRVLVNSASA QKRSKIPRSQ GCSREASPSR LSVARSSRIP RPSVSQGCSR EASRESSRDT
SPVRSFQPLA SRHHSRSTGA LYAPEVYGAS GPGYGISQSS RLSSSVSAMR VLNTGSDVEE
AVADALKKPA RRRYESYGMH SDDDANSDAS SACSERSYSS RNGSIPTYMR QTEDVAEVLN
RCASSNWSER KEGLLGLQNL LKNQRTLSRV ELKRLCEIFT RMFADPHGKR VFSMFLETLV
DFIQVHKDDL QDWLFVLLTQ LLKKMGADLL GSVQAKVQKA LDVTRESFPN DLQFNILMRF
TVDQTQTPSL KVKVAILKYI ETLAKQMDPG DFINSSETRL AVSRVITWTT EPKSSDVRKA
AQSVLISLFE LNTPEFTMLL GALPKTFQDG ATKLLHNHLR NTGNGTQSSM GSPLTRPTPR
SPANWSSPLT SPTNTSQNTL SPSAFDYDTE NMNSEDIYSS LRGVTEAIQN FSFRSQEDMN
EPLKRDSKKD DGDSMCGGPG MSDPRAGGDA TDSSQTALDN KASLLHSMPT HSSPRSRDYN
PYNYSDSISP FNKSALKEAM FDDDADQFPD DLSLDHSDLV AELLKELSNH NERVEERKIA
LYELMKLTQE ESFSVWDEHF KTILLLLLET LGDKEPTIRA LALKVLREIL RHQPARFKNY
AELTVMKTLE AHKDPHKEVV RSAEEAASVL ATSISPEQCI KVLCPIIQTA DYPINLAAIK
MQTKVIERVS KETLNLLLPE IMPGLIQGYD NSESSVRKAC VFCLVAVHAV IGDELKPHLS
QLTGSKMKLL NLYIKRAQTG SGGADPTTDV SGQS
