MARE2_HUMAN
ID MARE2_HUMAN Reviewed; 327 AA.
AC Q15555; B2RE21; B3KR39; B4DJV4; B7Z2L3; E9PHR3; F5H1V8; G5E9I6; Q9UQ33;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
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; Synonyms=RP1;
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), INDUCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH APC.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Oishi N.;
RT "RP1, a member of the APC-binding EB1 family, alternative form.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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 MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC TISSUE=Amygdala, Brain, and Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 [9]
RP INTERACTION WITH TUBULIN, AND SUBCELLULAR LOCATION.
RX PubMed=10188731;
RX DOI=10.1002/(sici)1097-0215(19990412)81:2<275::aid-ijc18>3.0.co;2-z;
RA Juwana J.-P., Henderikx P., Mischo A., Wadle A., Fadle N., Gerlach K.,
RA Arends J.W., Hoogenboom H., Pfreundschuh M., Renner C.;
RT "EB/RP gene family encodes tubulin binding proteins.";
RL Int. J. Cancer 81:275-284(1999).
RN [10]
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-167, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP 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 [15]
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 [16]
RP IDENTIFICATION BY 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 [17]
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 [18]
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).
RN [19]
RP 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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 5), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 5), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP 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 [22]
RP INVOLVEMENT IN CSCSC2, VARIANTS CSCSC2 SER-68; CYS-87 AND CYS-143,
RP CHARACTERIZATION OF VARIANTS CSCSC2 SER-68; CYS-87 AND CYS-143, AND
RP INTERACTION WITH TUBULIN.
RX PubMed=26637975; DOI=10.1016/j.ajhg.2015.10.014;
RA Isrie M., Breuss M., Tian G., Hansen A.H., Cristofoli F., Morandell J.,
RA Kupchinsky Z.A., Sifrim A., Rodriguez-Rodriguez C.M., Dapena E.P.,
RA Doonanco K., Leonard N., Tinsa F., Moortgat S., Ulucan H., Koparir E.,
RA Karaca E., Katsanis N., Marton V., Vermeesch J.R., Davis E.E., Cowan N.J.,
RA Keays D.A., Van Esch H.;
RT "Mutations in Either TUBB or MAPRE2 Cause Circumferential Skin Creases
RT Kunze Type.";
RL Am. J. Hum. Genet. 97:790-800(2015).
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 (PubMed:14514668). Interacts with APC
CC (via C-terminal) (PubMed:9233623, PubMed:14514668). Interacts with
CC monomeric and polymerized tubulin (PubMed:10188731, PubMed:14514668,
CC PubMed:26637975). Interacts with SLAIN1 (PubMed:21646404).
CC {ECO:0000269|PubMed:10188731, ECO:0000269|PubMed:14514668,
CC ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:26637975,
CC ECO:0000269|PubMed:9233623}.
CC -!- INTERACTION:
CC Q15555; Q9NQ79: CRTAC1; NbExp=7; IntAct=EBI-739717, EBI-10205543;
CC Q15555; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-739717, EBI-742054;
CC Q15555; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-739717, EBI-7960826;
CC Q15555; P25791: LMO2; NbExp=5; IntAct=EBI-739717, EBI-739696;
CC Q15555; P25791-3: LMO2; NbExp=7; IntAct=EBI-739717, EBI-11959475;
CC Q15555; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-739717, EBI-739832;
CC Q15555; Q15691: MAPRE1; NbExp=8; IntAct=EBI-739717, EBI-1004115;
CC Q15555; Q15555: MAPRE2; NbExp=5; IntAct=EBI-739717, EBI-739717;
CC Q15555; Q9UPY8: MAPRE3; NbExp=7; IntAct=EBI-739717, EBI-726739;
CC Q15555; Q6ZW49-2: PAXIP1; NbExp=3; IntAct=EBI-739717, EBI-10236271;
CC Q15555; P78332-2: RBM6; NbExp=3; IntAct=EBI-739717, EBI-14150298;
CC Q15555; Q13077: TRAF1; NbExp=9; IntAct=EBI-739717, EBI-359224;
CC Q15555; Q9BWF2: TRAIP; NbExp=10; IntAct=EBI-739717, EBI-1756205;
CC Q15555; Q99757: TXN2; NbExp=6; IntAct=EBI-739717, EBI-2932492;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10188731}. Note=Associated with the microtubule
CC network. Accumulates at the plus end of microtubules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q15555-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15555-2; Sequence=VSP_012944, VSP_012945;
CC Name=3;
CC IsoId=Q15555-3; Sequence=VSP_045710;
CC Name=5;
CC IsoId=Q15555-5; Sequence=VSP_055671;
CC Name=4;
CC IsoId=Q15555-4; Sequence=VSP_046041;
CC -!- TISSUE SPECIFICITY: Expressed in different tumor cell lines. Up-
CC regulated in activated B- and T-lymphocytes.
CC {ECO:0000269|PubMed:9233623}.
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.
CC -!- DISEASE: Skin creases, congenital symmetric circumferential, 2 (CSCSC2)
CC [MIM:616734]: An autosomal dominant disease characterized by multiple,
CC symmetric, circumferential rings of folded skin, affecting primarily
CC the limbs. Affected individuals also exhibit intellectual disability,
CC cleft palate, and dysmorphic features. {ECO:0000269|PubMed:26637975}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83375.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X94232; CAA63923.1; -; mRNA.
DR EMBL; AB016823; BAA83375.1; ALT_INIT; mRNA.
DR EMBL; CR536545; CAG38782.1; -; mRNA.
DR EMBL; BT020086; AAV38889.1; -; mRNA.
DR EMBL; AK090945; BAG52251.1; -; mRNA.
DR EMBL; AK296251; BAG58966.1; -; mRNA.
DR EMBL; AK294833; BAH11899.1; -; mRNA.
DR EMBL; AK315766; BAG38118.1; -; mRNA.
DR EMBL; AC009277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471088; EAX01336.1; -; Genomic_DNA.
DR EMBL; CH471088; EAX01338.1; -; Genomic_DNA.
DR EMBL; BC007318; AAH07318.1; -; mRNA.
DR CCDS; CCDS11910.1; -. [Q15555-1]
DR CCDS; CCDS45850.1; -. [Q15555-3]
DR CCDS; CCDS45851.1; -. [Q15555-5]
DR CCDS; CCDS58619.1; -. [Q15555-4]
DR PIR; G01037; G01037.
DR RefSeq; NP_001137298.1; NM_001143826.2. [Q15555-5]
DR RefSeq; NP_001137299.1; NM_001143827.2. [Q15555-3]
DR RefSeq; NP_001243349.1; NM_001256420.1. [Q15555-4]
DR RefSeq; NP_055083.1; NM_014268.3. [Q15555-1]
DR AlphaFoldDB; Q15555; -.
DR SMR; Q15555; -.
DR BioGRID; 116178; 105.
DR IntAct; Q15555; 35.
DR MINT; Q15555; -.
DR STRING; 9606.ENSP00000300249; -.
DR Allergome; 8363; Hom s RP1.
DR GlyGen; Q15555; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15555; -.
DR PhosphoSitePlus; Q15555; -.
DR BioMuta; MAPRE2; -.
DR DMDM; 60390165; -.
DR OGP; Q15555; -.
DR EPD; Q15555; -.
DR jPOST; Q15555; -.
DR MassIVE; Q15555; -.
DR MaxQB; Q15555; -.
DR PaxDb; Q15555; -.
DR PeptideAtlas; Q15555; -.
DR PRIDE; Q15555; -.
DR ProteomicsDB; 20585; -.
DR ProteomicsDB; 25777; -.
DR ProteomicsDB; 33949; -.
DR ProteomicsDB; 60631; -. [Q15555-1]
DR ProteomicsDB; 60632; -. [Q15555-2]
DR Antibodypedia; 8544; 430 antibodies from 31 providers.
DR DNASU; 10982; -.
DR Ensembl; ENST00000300249.10; ENSP00000300249.4; ENSG00000166974.13. [Q15555-1]
DR Ensembl; ENST00000413393.5; ENSP00000396074.1; ENSG00000166974.13. [Q15555-5]
DR Ensembl; ENST00000436190.6; ENSP00000407723.1; ENSG00000166974.13. [Q15555-3]
DR Ensembl; ENST00000538170.6; ENSP00000446343.1; ENSG00000166974.13. [Q15555-4]
DR Ensembl; ENST00000588910.5; ENSP00000468588.1; ENSG00000166974.13. [Q15555-2]
DR Ensembl; ENST00000589699.1; ENSP00000464921.1; ENSG00000166974.13. [Q15555-5]
DR GeneID; 10982; -.
DR KEGG; hsa:10982; -.
DR MANE-Select; ENST00000300249.10; ENSP00000300249.4; NM_014268.4; NP_055083.1.
DR UCSC; uc002kyf.3; human. [Q15555-1]
DR CTD; 10982; -.
DR DisGeNET; 10982; -.
DR GeneCards; MAPRE2; -.
DR HGNC; HGNC:6891; MAPRE2.
DR HPA; ENSG00000166974; Low tissue specificity.
DR MalaCards; MAPRE2; -.
DR MIM; 605789; gene.
DR MIM; 616734; phenotype.
DR neXtProt; NX_Q15555; -.
DR OpenTargets; ENSG00000166974; -.
DR Orphanet; 2505; Multiple benign circumferential skin creases on limbs.
DR PharmGKB; PA30635; -.
DR VEuPathDB; HostDB:ENSG00000166974; -.
DR eggNOG; KOG3000; Eukaryota.
DR GeneTree; ENSGT00490000043329; -.
DR HOGENOM; CLU_041744_1_0_1; -.
DR InParanoid; Q15555; -.
DR OMA; EQCGTGG; -.
DR PhylomeDB; Q15555; -.
DR TreeFam; TF313620; -.
DR PathwayCommons; Q15555; -.
DR SignaLink; Q15555; -.
DR BioGRID-ORCS; 10982; 8 hits in 1079 CRISPR screens.
DR ChiTaRS; MAPRE2; human.
DR GeneWiki; MAPRE2; -.
DR GenomeRNAi; 10982; -.
DR Pharos; Q15555; Tbio.
DR PRO; PR:Q15555; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q15555; protein.
DR Bgee; ENSG00000166974; Expressed in cortical plate and 211 other tissues.
DR ExpressionAtlas; Q15555; baseline and differential.
DR Genevisible; Q15555; HS.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
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; IDA:LIFEdb.
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; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IDA:ARUK-UCL.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032014; P:positive regulation of ARF protein signal transduction; ISS:ARUK-UCL.
DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; ISS:ARUK-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:ARUK-UCL.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; ISS: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 Acetylation; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..327
FT /note="Microtubule-associated protein RP/EB family member
FT 2"
FT /id="PRO_0000213424"
FT DOMAIN 57..159
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 236..306
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..327
FT /note="DCTN1-binding"
FT REGION 259..302
FT /note="APC-binding"
FT REGION 299..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 167
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..83
FT /note="MPGPTQTLSPNGENNNDIIQDNNGTIIPFRKHTVRGERSYSWGMAVNVYSTS
FT ITQETMSRHDIIAWVNDIVSLNYTKVEQLCS -> MARTTTTSSRIITGPSFLSGSTQC
FT AGSVPT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046041"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055671"
FT VAR_SEQ 1..40
FT /note="MPGPTQTLSPNGENNNDIIQDNNGTIIPFRKHTVRGERSY -> MKQNRDQK
FT CPVSQRNSSFQQPGRKPGCS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045710"
FT VAR_SEQ 252..259
FT /note="HSLKLALE -> MHQLWPRL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012944"
FT VAR_SEQ 260..327
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012945"
FT VARIANT 68
FT /note="N -> S (in CSCSC2; enhances binding to microtubules;
FT dbSNP:rs864309719)"
FT /evidence="ECO:0000269|PubMed:26637975"
FT /id="VAR_076540"
FT VARIANT 87
FT /note="Y -> C (in CSCSC2; enhances binding to microtubules;
FT dbSNP:rs864309717)"
FT /evidence="ECO:0000269|PubMed:26637975"
FT /id="VAR_076541"
FT VARIANT 143
FT /note="R -> C (in CSCSC2; enhances binding to microtubules;
FT dbSNP:rs864309720)"
FT /evidence="ECO:0000269|PubMed:26637975"
FT /id="VAR_076542"
FT VARIANT 162
FT /note="Y -> C (in dbSNP:rs11538993)"
FT /id="VAR_050018"
FT CONFLICT 65
FT /note="A -> G (in Ref. 8; BAA83375)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="S -> N (in Ref. 5; BAG58966)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="M -> K (in Ref. 5; BAG58966)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="S -> G (in Ref. 5; BAG52251)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="K -> I (in Ref. 5; BAH11899)"
FT /evidence="ECO:0000305"
FT INIT_MET Q15555-5:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q15555-5:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 327 AA; 37031 MW; 2BE99E9F9EFA83C3 CRC64;
MPGPTQTLSP NGENNNDIIQ DNNGTIIPFR KHTVRGERSY SWGMAVNVYS TSITQETMSR
HDIIAWVNDI VSLNYTKVEQ LCSGAAYCQF MDMLFPGCIS LKKVKFQAKL EHEYIHNFKL
LQASFKRMNV DKVIPVEKLV KGRFQDNLDF IQWFKKFYDA NYDGKEYDPV EARQGQDAIP
PPDPGEQIFN LPKKSHHANS PTAGAAKSSP AAKPGSTPSR PSSAKRASSS GSASKSDKDL
ETQVIQLNEQ VHSLKLALEG VEKERDFYFG KLREIELLCQ EHGQENDDLV QRLMDILYAS
EEHEGHTEEP EAEEQAHEQQ PPQQEEY
