MARE2_MOUSE
ID MARE2_MOUSE Reviewed; 326 AA.
AC Q8R001; Q3UF61; Q8BLZ6; Q8BYR6; Q8C177; Q8K109;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Microtubule-associated protein RP/EB family member 2;
DE AltName: Full=APC-binding protein EB2;
DE AltName: Full=End-binding protein 2;
DE Short=EB2;
GN Name=Mapre2;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Aorta, Corpora quadrigemina, Hypothalamus, Skin,
RC Sympathetic ganglion, and Vein;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Eye, and Liver;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [5]
RP INTERACTION WITH 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).
CC -!- FUNCTION: May be involved in microtubule polymerization, and spindle
CC function by stabilizing microtubules and anchoring them at centrosomes.
CC May play a role in cell migration (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DCTN1. Interacts with APC (via C-terminal).
CC Interacts with monomeric and polymerized tubulin (By similarity).
CC Interacts with SLAIN1 (PubMed:21646404). {ECO:0000250|UniProtKB:Q15555,
CC ECO:0000269|PubMed:21646404}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Associated with the microtubule network.
CC Accumulates at the plus end of microtubules (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R001-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R001-2; Sequence=VSP_012946;
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
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DR EMBL; AK028823; BAC26138.1; -; mRNA.
DR EMBL; AK038562; BAC30045.1; -; mRNA.
DR EMBL; AK040767; BAC30700.1; -; mRNA.
DR EMBL; AK045493; BAC32393.1; -; mRNA.
DR EMBL; AK045904; BAE43326.1; -; mRNA.
DR EMBL; AK046221; BAC32643.1; -; mRNA.
DR EMBL; AK148954; BAE28700.1; -; mRNA.
DR EMBL; BC025804; AAH25804.1; -; mRNA.
DR EMBL; BC027056; AAH27056.1; -; mRNA.
DR EMBL; BC028987; AAH28987.1; -; mRNA.
DR EMBL; BC035254; AAH35254.1; -; mRNA.
DR CCDS; CCDS29095.1; -. [Q8R001-1]
DR CCDS; CCDS50237.1; -. [Q8R001-2]
DR RefSeq; NP_001156413.1; NM_001162941.1. [Q8R001-2]
DR RefSeq; NP_001156414.1; NM_001162942.1.
DR RefSeq; NP_694698.3; NM_153058.4. [Q8R001-1]
DR AlphaFoldDB; Q8R001; -.
DR SMR; Q8R001; -.
DR BioGRID; 229310; 13.
DR IntAct; Q8R001; 3.
DR MINT; Q8R001; -.
DR STRING; 10090.ENSMUSP00000025127; -.
DR iPTMnet; Q8R001; -.
DR PhosphoSitePlus; Q8R001; -.
DR EPD; Q8R001; -.
DR jPOST; Q8R001; -.
DR MaxQB; Q8R001; -.
DR PaxDb; Q8R001; -.
DR PeptideAtlas; Q8R001; -.
DR PRIDE; Q8R001; -.
DR ProteomicsDB; 292086; -. [Q8R001-1]
DR ProteomicsDB; 292087; -. [Q8R001-2]
DR Antibodypedia; 8544; 430 antibodies from 31 providers.
DR DNASU; 212307; -.
DR Ensembl; ENSMUST00000025127; ENSMUSP00000025127; ENSMUSG00000024277. [Q8R001-1]
DR Ensembl; ENSMUST00000115830; ENSMUSP00000111496; ENSMUSG00000024277. [Q8R001-2]
DR GeneID; 212307; -.
DR KEGG; mmu:212307; -.
DR UCSC; uc008ege.2; mouse. [Q8R001-2]
DR UCSC; uc008egf.2; mouse. [Q8R001-1]
DR CTD; 10982; -.
DR MGI; MGI:106271; Mapre2.
DR VEuPathDB; HostDB:ENSMUSG00000024277; -.
DR eggNOG; KOG3000; Eukaryota.
DR GeneTree; ENSGT00490000043329; -.
DR InParanoid; Q8R001; -.
DR OMA; EQCGTGG; -.
DR OrthoDB; 1237523at2759; -.
DR PhylomeDB; Q8R001; -.
DR TreeFam; TF313620; -.
DR BioGRID-ORCS; 212307; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Mapre2; mouse.
DR PRO; PR:Q8R001; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8R001; protein.
DR Bgee; ENSMUSG00000024277; Expressed in rostral migratory stream and 259 other tissues.
DR ExpressionAtlas; Q8R001; baseline and differential.
DR Genevisible; Q8R001; MM.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:ARUK-UCL.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
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:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032014; P:positive regulation of ARF protein signal transduction; IMP:ARUK-UCL.
DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; IMP:ARUK-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:ARUK-UCL.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IMP:ARUK-UCL.
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 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; IPR027328; MAPRE.
DR InterPro; IPR027735; RP1/EB2_vertebrate.
DR PANTHER; PTHR10623; PTHR10623; 1.
DR PANTHER; PTHR10623:SF7; PTHR10623:SF7; 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 Alternative splicing; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..326
FT /note="Microtubule-associated protein RP/EB family member
FT 2"
FT /id="PRO_0000213425"
FT DOMAIN 56..158
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 235..305
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 170..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..326
FT /note="DCTN1-binding"
FT /evidence="ECO:0000250"
FT REGION 258..301
FT /note="APC-binding"
FT /evidence="ECO:0000250"
FT REGION 297..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15555"
FT MOD_RES 166
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15555"
FT VAR_SEQ 1..40
FT /note="MPGPTQTLSPNGENNNDIIQDNGTIIPFRKHTVRGERSYS -> MKQIRDQR
FT VIRKGPQKHHSLQQPGRVPGCSN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012946"
FT CONFLICT 103
FT /note="V -> E (in Ref. 1; BAC30045)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="H -> Y (in Ref. 2; AAH35254/AAH28987)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="Q -> H (in Ref. 1; BAC30700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 36946 MW; 51C0916F37075651 CRC64;
MPGPTQTLSP NGENNNDIIQ DNGTIIPFRK HTVRGERSYS WGMAVNVYST SITQETMSRH
DIIAWVNDIV SLNYTKVEQL CSGAAYCQFM DMLFPGCISL KKVKFQAKLE HEYIHNFKLL
QASFKRMNVD KVIPVEKLVK GRFQDNLDFI QWFKKFYDAN YDGKEYDPVE ARQGQDAIPP
PDPGEQIFNL PKKSHHANSP TAGAAKSSPA SKPGSTPSRP SSAKRASSSG SASRSDKDLE
TQVIQLNEQV HSLKLALEGV EKERDFYFGK LREIELLCQE HGQENDDLVQ RLMEVLYASD
EQEGQTEEPE AEEQAHDQQP QQQEEY
