CLAP2_MOUSE
ID CLAP2_MOUSE Reviewed; 1286 AA.
AC Q8BRT1; Q8CHE3; Q99JI3; Q9DB80;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=CLIP-associating protein 2;
DE AltName: Full=Cytoplasmic linker-associated protein 2;
GN Name=Clasp2; Synonyms=Kiaa0627;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, ALTERNATIVE
RP SPLICING, TISSUE SPECIFICITY, INTERACTION WITH CLIP2 AND RSN, AND
RP MUTAGENESIS OF CYS-6 AND CYS-10.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
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 [LARGE SCALE MRNA] OF 90-1286 (ISOFORM 1).
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [5]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16123238; DOI=10.1530/rep.1.00651;
RA Moore C.A., Zernicka-Goetz M.;
RT "PAR-1 and the microtubule-associated proteins CLASP2 and dynactin-p50 have
RT specific localisation on mouse meiotic and first mitotic spindles.";
RL Reproduction 130:311-320(2005).
RN [8]
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 [9]
RP INTERACTION WITH MACF1.
RX PubMed=18854161; DOI=10.1016/j.cell.2008.07.045;
RA Wu X., Kodama A., Fuchs E.;
RT "ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has
RT ATPase activity.";
RL Cell 135:137-148(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-374; SER-376; SER-620
RP AND SER-947, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 642-873, AND DOMAIN.
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. Involved in the nucleation of
CC noncentrosomal microtubules originating from the trans-Golgi network
CC (TGN). Required for the polarization of the cytoplasmic microtubule
CC arrays in migrating cells towards the leading edge of the cell. May act
CC at the cell cortex to enhance the frequency of rescue of depolymerizing
CC microtubules by attaching their plus-ends to cortical platforms
CC composed of ERC1 and PHLDB2. This cortical microtubule stabilizing
CC activity is regulated at least in part by phosphatidylinositol 3-kinase
CC signaling. Also performs a similar stabilizing function at the
CC kinetochore which is essential for the bipolar alignment of chromosomes
CC on the mitotic spindle. Acts as a mediator of ERBB2-dependent
CC stabilization of microtubules at the cell cortex.
CC {ECO:0000250|UniProtKB:O75122, ECO:0000269|PubMed:16914514}.
CC -!- SUBUNIT: Interacts with microtubules (PubMed:11290329). Interacts with
CC MAPRE1; probably required for targeting to growing microtubule plus
CC ends. Interacts with ERC1, MAPRE3 and PHLDB2. The interaction with ERC1
CC may be mediated by PHLDB2. Interacts with GCC2; recruits CLASP2 to
CC Golgi membranes (By similarity). Interacts with CLIP2 and RSN
CC (PubMed:11290329). Interacts with MACF1 (PubMed:18854161).
CC {ECO:0000250|UniProtKB:O75122, ECO:0000269|PubMed:11290329,
CC ECO:0000269|PubMed:18854161}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11290329}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Chromosome, centromere, kinetochore.
CC Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle
CC pole. Golgi apparatus {ECO:0000269|PubMed:11290329}. Golgi apparatus,
CC trans-Golgi network {ECO:0000250|UniProtKB:O75122}. Cell membrane
CC {ECO:0000250|UniProtKB:O75122}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:O75122}. Note=Localizes to microtubule plus ends
CC (PubMed:11290329). 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. In
CC migrating cells localizes to the plus ends of microtubules within the
CC cell body and to the entire microtubule lattice within the lamella.
CC Localizes to the cell cortex and this requires ERC1 and PHLDB2 (By
CC similarity). Also localizes to meiotic spindle poles. The MEMO1-RHOA-
CC DIAPH1 signaling pathway controls localization of the phosphorylated
CC form to the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:O75122, ECO:0000269|PubMed:11290329}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BRT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BRT1-5; Sequence=VSP_015808, VSP_015811;
CC Name=3;
CC IsoId=Q8BRT1-6; Sequence=VSP_015809, VSP_015810, VSP_015812;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and at low levels in
CC heart, kidney and lung. {ECO:0000269|PubMed:11290329}.
CC -!- DEVELOPMENTAL STAGE: Expressed in oocytes and early embryos.
CC {ECO:0000269|PubMed:16123238}.
CC -!- DOMAIN: The two SXIP sequence motifs mediate interaction with MAPRE1;
CC this is necessary for targeting to growing microtubule plus ends.
CC {ECO:0000250|UniProtKB:O75122}.
CC -!- DOMAIN: Two TOG regions display structural characteristics similar to
CC HEAT repeat domains and mediate interaction with microtubules.
CC {ECO:0000250|UniProtKB:O75122, ECO:0000269|PubMed:26003921}.
CC -!- PTM: Phosphorylated by GSK3B. Phosphorylation by GSK3B may negatively
CC regulate binding to microtubule lattices in lamella. Isoform 2 is
CC phosphorylated on Ser-241.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41436.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ276961; CAC35161.1; -; mRNA.
DR EMBL; AK043551; BAC31579.1; -; mRNA.
DR EMBL; AK005146; BAB23842.1; -; mRNA.
DR EMBL; BC030468; AAH30468.1; -; mRNA.
DR EMBL; AB093252; BAC41436.2; ALT_FRAME; Transcribed_RNA.
DR CCDS; CCDS52948.1; -. [Q8BRT1-1]
DR RefSeq; NP_001273528.1; NM_001286599.1.
DR RefSeq; NP_001273529.1; NM_001286600.1.
DR RefSeq; NP_001273530.1; NM_001286601.1.
DR RefSeq; NP_001273531.1; NM_001286602.1.
DR RefSeq; NP_001273532.1; NM_001286603.1. [Q8BRT1-6]
DR PDB; 3WOZ; X-ray; 2.20 A; A/B/C/D=642-873.
DR PDBsum; 3WOZ; -.
DR AlphaFoldDB; Q8BRT1; -.
DR SMR; Q8BRT1; -.
DR BioGRID; 218155; 27.
DR IntAct; Q8BRT1; 7.
DR MINT; Q8BRT1; -.
DR STRING; 10090.ENSMUSP00000128460; -.
DR iPTMnet; Q8BRT1; -.
DR PhosphoSitePlus; Q8BRT1; -.
DR SwissPalm; Q8BRT1; -.
DR EPD; Q8BRT1; -.
DR jPOST; Q8BRT1; -.
DR MaxQB; Q8BRT1; -.
DR PaxDb; Q8BRT1; -.
DR PeptideAtlas; Q8BRT1; -.
DR PRIDE; Q8BRT1; -.
DR ProteomicsDB; 283517; -. [Q8BRT1-1]
DR ProteomicsDB; 283518; -. [Q8BRT1-5]
DR ProteomicsDB; 283519; -. [Q8BRT1-6]
DR DNASU; 76499; -.
DR GeneID; 76499; -.
DR KEGG; mmu:76499; -.
DR UCSC; uc009rwt.2; mouse. [Q8BRT1-6]
DR CTD; 23122; -.
DR MGI; MGI:1923749; Clasp2.
DR eggNOG; KOG2956; Eukaryota.
DR InParanoid; Q8BRT1; -.
DR OrthoDB; 66632at2759; -.
DR PhylomeDB; Q8BRT1; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 76499; 9 hits in 70 CRISPR screens.
DR ChiTaRS; Clasp2; mouse.
DR PRO; PR:Q8BRT1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BRT1; protein.
DR GO; GO:0044295; C:axonal growth cone; ISO:MGI.
DR GO; GO:0045180; C:basal cortex; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:1903754; C:cortical microtubule plus-end; ISO:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0002162; F:dystroglycan binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034453; P:microtubule anchoring; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; IMP:MGI.
DR GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; ISO:MGI.
DR GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; ISO:MGI.
DR GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; ISO:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISO:MGI.
DR GO; GO:1905477; P:positive regulation of protein localization to membrane; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0030516; P:regulation of axon extension; ISO:MGI.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0010470; P:regulation of gastrulation; ISO:MGI.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISO:MGI.
DR GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
DR GO; GO:0006903; P:vesicle targeting; ISO:MGI.
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; 2.
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; Meiosis; Membrane; Microtubule;
KW Mitosis; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1286
FT /note="CLIP-associating protein 2"
FT /id="PRO_0000089850"
FT REPEAT 179..214
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 215..251
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 256..293
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 702..739
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 764..801
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 1046..1083
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 1090..1127
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 1208..1245
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REGION 1..40
FT /note="Golgi localization"
FT REGION 17..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..317
FT /note="TOG 1"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT REGION 320..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..565
FT /note="Interaction with microtubules, MAPRE1 and MAPRE3"
FT /evidence="ECO:0000250"
FT REGION 493..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..873
FT /note="TOG 2"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT REGION 864..1286
FT /note="Interaction with RSN and localization to the Golgi
FT and kinetochores"
FT /evidence="ECO:0000250"
FT REGION 870..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1286
FT /note="Required for cortical localization"
FT /evidence="ECO:0000250"
FT MOTIF 500..503
FT /note="SXIP motif 1; mediates interaction with MAPRE1 and
FT targeting to microtubule plus ends"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOTIF 523..526
FT /note="SXIP motif 2; mediates interaction with MAPRE1 and
FT targeting to microtubule plus ends"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT COMPBIAS 320..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JD4"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JD4"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 779
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 944
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1005
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT VAR_SEQ 1..12
FT /note="MRRLICKRICDY -> MEPRGAEYFCAQVLQKDVSGRLQAGEELLLCLGTPG
FT AIPDLEDDPSRLAKTVDALTRWVGSSNYRVSLLGLEILSAFVDRLSTRFKSYVTMVTTA
FT LIDRMGDVKDKVREEAQNLTLKLMDEVAPPMYIWEQLASGFKHKNFRSREGVCLCLIET
FT LNIFGTQPLVISKLVPHLCVLFGDSNSQVRNAALSAVVEIYRHVGEKLRIDLCKRDIPP
FT ARLEMVLAKFDEVQNSGGMILSVCKD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11290329"
FT /id="VSP_015808"
FT VAR_SEQ 1..12
FT /note="MRRLICKRICDY -> MAMGDD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015809"
FT VAR_SEQ 119..173
FT /note="LKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVVREACITVAHLS
FT TVL -> CMSCSLVASEVERALAWPLWSHLATYQHHCHCTLSHEDLPEKRLTSPVSSAF
FT VQH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015810"
FT VAR_SEQ 142..1054
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11290329"
FT /id="VSP_015811"
FT VAR_SEQ 174..1286
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015812"
FT MUTAGEN 6
FT /note="C->S: Impairs Golgi localization; when associated
FT with S-10."
FT /evidence="ECO:0000269|PubMed:11290329"
FT MUTAGEN 10
FT /note="C->S: Impairs Golgi localization; when associated
FT with S-6."
FT /evidence="ECO:0000269|PubMed:11290329"
FT CONFLICT 657
FT /note="S -> T (in Ref. 4; BAC41436)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="I -> V (in Ref. 4; BAC41436)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="P -> L (in Ref. 4; BAC41436)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="K -> KR (in Ref. 4; BAC41436)"
FT /evidence="ECO:0000305"
FT HELIX 648..655
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 660..675
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 682..695
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 701..718
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 719..721
FT /evidence="ECO:0007829|PDB:3WOZ"
FT TURN 723..725
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 726..737
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 743..759
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 762..774
FT /evidence="ECO:0007829|PDB:3WOZ"
FT STRAND 776..778
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 782..796
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 801..803
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 808..820
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 827..843
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 845..853
FT /evidence="ECO:0007829|PDB:3WOZ"
FT HELIX 857..867
FT /evidence="ECO:0007829|PDB:3WOZ"
SQ SEQUENCE 1286 AA; 140739 MW; 5B208D8F4E90CB93 CRC64;
MRRLICKRIC DYKSFDDEES VDGNRPSSAA SAFKVPAPKT PGNPVSSARK PGSAGGPKVG
GPSKEGGAGA VDEDDFIKAF TDVPSVQIYS SRELEETLNK IREILSDDKH DWDQRANALK
KIRSLLVAGA AQYDCFFQHL RLLDGALKLS AKDLRSQVVR EACITVAHLS TVLGNKFDHG
AEAIVPTLFN LVPNSAKVMA TSGCAAIRFI IRHTHVPRLI PLITSNCTSK SVPVRRRSFE
FLDLLLQEWQ THSLERHAAV LVETIKKGIH DADAEARVEA RKTYMGLRNH FPGEAETLYN
SLEPSYQKSL QTYLKSSGSV ASLPQSDRSS SSSQESLNRP FSSKWSTANP STVAGRVSVG
GSKANPLPGS LQRSRSDIDV NAAAGAKAHH AAGQAVRSGR LGAGALNPGS YASLEDTSDK
MDGTASDDGR VRAKLSTPLV AVGNAKTDSR GRSRTKMVSQ SQPGSRSGSP GRVLTTTALS
TVSSGAQRVL VNSASAQKRS KIPRSQGCSR EASPSRLSVA RSSRIPRPSV SQGCSREASR
ESSRDTSPVR SFQPLGPGYG ISQSSRLSSS VSAMRVLNTG SDVEEAVADA LLLGDIRTKK
KPARRRYESY GMHSDDDANS DASSACSERS YSSRNGSIPT YMRQTEDVAE VLNRCASSNW
SERKEGLLGL QNLLKNQRTL SRIELKRLCE IFTRMFADPH GKVFSMFLET LVDFIQVHKD
DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ KALDITRESF PNDLQFNILM RFTVDQTQTP
SLKVKVAILK YIETLAKQMD PRDFTNSSET RLAVSRVITW TTEPKSSDVR KAAQSVLISL
FELNTPEFTM LLGALPKTFQ DGATKLLHNH LRNTGNGTQS SMGSPLTRPT PRSPANWSSP
LTSPTNTSQN TLSPSAFDYD TENMNSEDIY SSLRGVTEAI QNFSFRSQED MSEPVRRDPK
KEDGDTICSG PGMSDPRAGG DAADGSQPAL DNKASLLHSM PLHSSPRSRD YNPYNYSDSI
SPFNKSALKE AMFDDDADQF PDDLSLDHSD LVAELLKELS NHNERIEERK IALYELMKLT
QEESFSVWDE HFKTILLLLL ETLGDKEPTI RALALKVLKE ILRHQPARFK NYAELTVMKT
LEAHKDPHKE VVRSAEEAAS VLATSISPEQ CIKVLCPIIQ TADYPINLAA IKMQTKVIER
VSKETLNMLL PEIMPGLIQG YDNSESSVRK ACVFCLVAVH AVIGDELKPH LSQLTGSKMK
LLNLYIKRAQ TGSAGADPTA DVSGQS
