Full text data of MAPRE2
MAPRE2
(RP1)
[Confidence: low (only semi-automatic identification from reviews)]
Microtubule-associated protein RP/EB family member 2 (APC-binding protein EB2; End-binding protein 2; EB2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Microtubule-associated protein RP/EB family member 2 (APC-binding protein EB2; End-binding protein 2; EB2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15555
ID MARE2_HUMAN Reviewed; 327 AA.
AC Q15555; B2RE21; B3KR39; B7Z2L3; E9PHR3; F5H1V8; Q9UQ33;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 120.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH APC.
RX PubMed=9233623;
RA Renner C., Pfitzenmeier J.-P., Gerlach K., Held G., Ohnesorge S.,
RA Sahin U., Bauer S., Pfreundschuh M.;
RT "RP1, a new member of the adenomatous polyposis coli-binding EB1-like
RT gene 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.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., 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
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT proteins.";
RL J. Biol. Chem. 278:49721-49731(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-167, AND MASS
RP SPECTROMETRY.
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
RT 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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 MASS
RP SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP IDENTIFICATION 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be involved in microtubule polymerization, and
CC spindle function by stabilizing microtubules and anchoring them at
CC centrosomes. May play a role in cell migration (By similarity).
CC -!- SUBUNIT: Interacts with DCTN1. Binds to the C-terminal domain of
CC APC. Binds monomeric and polymerized tubulin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Associated
CC with the microtubule network. Accumulates at the plus end of
CC microtubules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
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 Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q15555-4; Sequence=VSP_046041;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in different tumor cell lines. Up-
CC regulated in activated B- and T-lymphocytes.
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
CC mutually exclusive complexes with APC and DCTN1.
CC -!- SIMILARITY: Belongs to the MAPRE family.
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SIMILARITY: Contains 1 EB1 C-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83375.1; Type=Erroneous initiation;
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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; 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; BC007318; AAH07318.1; -; mRNA.
DR PIR; G01037; G01037.
DR RefSeq; NP_001137298.1; NM_001143826.2.
DR RefSeq; NP_001137299.1; NM_001143827.2.
DR RefSeq; NP_001243349.1; NM_001256420.1.
DR RefSeq; NP_055083.1; NM_014268.3.
DR UniGene; Hs.532824; -.
DR ProteinModelPortal; Q15555; -.
DR SMR; Q15555; 44-173, 246-302.
DR IntAct; Q15555; 8.
DR MINT; MINT-1458854; -.
DR STRING; 9606.ENSP00000300249; -.
DR Allergome; 8363; Hom s RP1.
DR PhosphoSite; Q15555; -.
DR DMDM; 60390165; -.
DR OGP; Q15555; -.
DR PaxDb; Q15555; -.
DR PeptideAtlas; Q15555; -.
DR PRIDE; Q15555; -.
DR DNASU; 10982; -.
DR Ensembl; ENST00000300249; ENSP00000300249; ENSG00000166974.
DR Ensembl; ENST00000436190; ENSP00000407723; ENSG00000166974.
DR Ensembl; ENST00000538170; ENSP00000446343; ENSG00000166974.
DR Ensembl; ENST00000588910; ENSP00000468588; ENSG00000166974.
DR GeneID; 10982; -.
DR KEGG; hsa:10982; -.
DR UCSC; uc002kyh.4; human.
DR CTD; 10982; -.
DR GeneCards; GC18P032556; -.
DR HGNC; HGNC:6891; MAPRE2.
DR HPA; HPA016738; -.
DR HPA; HPA016739; -.
DR MIM; 605789; gene.
DR neXtProt; NX_Q15555; -.
DR PharmGKB; PA30635; -.
DR eggNOG; COG5217; -.
DR HOGENOM; HOG000198048; -.
DR HOVERGEN; HBG052410; -.
DR InParanoid; Q15555; -.
DR KO; K10436; -.
DR OMA; HESHTEE; -.
DR PhylomeDB; Q15555; -.
DR ChiTaRS; MAPRE2; human.
DR GeneWiki; MAPRE2; -.
DR GenomeRNAi; 10982; -.
DR NextBio; 41726; -.
DR PRO; PR:Q15555; -.
DR ArrayExpress; Q15555; -.
DR Bgee; Q15555; -.
DR CleanEx; HS_MAPRE2; -.
DR CleanEx; HS_RP1; -.
DR Genevestigator; Q15555; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:LIFEdb.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR004953; EB1_C.
DR InterPro; IPR027328; MAPRE.
DR InterPro; IPR027735; RP1/EB2.
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; Complete proteome;
KW Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 327 Microtubule-associated protein RP/EB
FT family member 2.
FT /FTId=PRO_0000213424.
FT DOMAIN 57 159 CH.
FT DOMAIN 236 306 EB1 C-terminal.
FT REGION 187 327 DCTN1-binding.
FT REGION 259 302 APC-binding.
FT MOD_RES 167 167 Phosphotyrosine.
FT MOD_RES 219 219 Phosphoserine.
FT VAR_SEQ 1 83 MPGPTQTLSPNGENNNDIIQDNNGTIIPFRKHTVRGERSYS
FT WGMAVNVYSTSITQETMSRHDIIAWVNDIVSLNYTKVEQLC
FT S -> MARTTTTSSRIITGPSFLSGSTQCAGSVPT (in
FT isoform 4).
FT /FTId=VSP_046041.
FT VAR_SEQ 1 40 MPGPTQTLSPNGENNNDIIQDNNGTIIPFRKHTVRGERSY
FT -> MKQNRDQKCPVSQRNSSFQQPGRKPGCS (in
FT isoform 3).
FT /FTId=VSP_045710.
FT VAR_SEQ 252 259 HSLKLALE -> MHQLWPRL (in isoform 2).
FT /FTId=VSP_012944.
FT VAR_SEQ 260 327 Missing (in isoform 2).
FT /FTId=VSP_012945.
FT VARIANT 162 162 Y -> C (in dbSNP:rs11538993).
FT /FTId=VAR_050018.
FT CONFLICT 65 65 A -> G (in Ref. 8; BAA83375).
FT CONFLICT 209 209 S -> G (in Ref. 5; BAG52251).
FT CONFLICT 235 235 K -> I (in Ref. 5; BAH11899).
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
//
ID MARE2_HUMAN Reviewed; 327 AA.
AC Q15555; B2RE21; B3KR39; B7Z2L3; E9PHR3; F5H1V8; Q9UQ33;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 120.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH APC.
RX PubMed=9233623;
RA Renner C., Pfitzenmeier J.-P., Gerlach K., Held G., Ohnesorge S.,
RA Sahin U., Bauer S., Pfreundschuh M.;
RT "RP1, a new member of the adenomatous polyposis coli-binding EB1-like
RT gene 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.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., 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
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT proteins.";
RL J. Biol. Chem. 278:49721-49731(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-167, AND MASS
RP SPECTROMETRY.
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
RT 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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 MASS
RP SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP IDENTIFICATION 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be involved in microtubule polymerization, and
CC spindle function by stabilizing microtubules and anchoring them at
CC centrosomes. May play a role in cell migration (By similarity).
CC -!- SUBUNIT: Interacts with DCTN1. Binds to the C-terminal domain of
CC APC. Binds monomeric and polymerized tubulin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Associated
CC with the microtubule network. Accumulates at the plus end of
CC microtubules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
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 Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q15555-4; Sequence=VSP_046041;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in different tumor cell lines. Up-
CC regulated in activated B- and T-lymphocytes.
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
CC mutually exclusive complexes with APC and DCTN1.
CC -!- SIMILARITY: Belongs to the MAPRE family.
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SIMILARITY: Contains 1 EB1 C-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83375.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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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; 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; BC007318; AAH07318.1; -; mRNA.
DR PIR; G01037; G01037.
DR RefSeq; NP_001137298.1; NM_001143826.2.
DR RefSeq; NP_001137299.1; NM_001143827.2.
DR RefSeq; NP_001243349.1; NM_001256420.1.
DR RefSeq; NP_055083.1; NM_014268.3.
DR UniGene; Hs.532824; -.
DR ProteinModelPortal; Q15555; -.
DR SMR; Q15555; 44-173, 246-302.
DR IntAct; Q15555; 8.
DR MINT; MINT-1458854; -.
DR STRING; 9606.ENSP00000300249; -.
DR Allergome; 8363; Hom s RP1.
DR PhosphoSite; Q15555; -.
DR DMDM; 60390165; -.
DR OGP; Q15555; -.
DR PaxDb; Q15555; -.
DR PeptideAtlas; Q15555; -.
DR PRIDE; Q15555; -.
DR DNASU; 10982; -.
DR Ensembl; ENST00000300249; ENSP00000300249; ENSG00000166974.
DR Ensembl; ENST00000436190; ENSP00000407723; ENSG00000166974.
DR Ensembl; ENST00000538170; ENSP00000446343; ENSG00000166974.
DR Ensembl; ENST00000588910; ENSP00000468588; ENSG00000166974.
DR GeneID; 10982; -.
DR KEGG; hsa:10982; -.
DR UCSC; uc002kyh.4; human.
DR CTD; 10982; -.
DR GeneCards; GC18P032556; -.
DR HGNC; HGNC:6891; MAPRE2.
DR HPA; HPA016738; -.
DR HPA; HPA016739; -.
DR MIM; 605789; gene.
DR neXtProt; NX_Q15555; -.
DR PharmGKB; PA30635; -.
DR eggNOG; COG5217; -.
DR HOGENOM; HOG000198048; -.
DR HOVERGEN; HBG052410; -.
DR InParanoid; Q15555; -.
DR KO; K10436; -.
DR OMA; HESHTEE; -.
DR PhylomeDB; Q15555; -.
DR ChiTaRS; MAPRE2; human.
DR GeneWiki; MAPRE2; -.
DR GenomeRNAi; 10982; -.
DR NextBio; 41726; -.
DR PRO; PR:Q15555; -.
DR ArrayExpress; Q15555; -.
DR Bgee; Q15555; -.
DR CleanEx; HS_MAPRE2; -.
DR CleanEx; HS_RP1; -.
DR Genevestigator; Q15555; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:LIFEdb.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR004953; EB1_C.
DR InterPro; IPR027328; MAPRE.
DR InterPro; IPR027735; RP1/EB2.
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; Complete proteome;
KW Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 327 Microtubule-associated protein RP/EB
FT family member 2.
FT /FTId=PRO_0000213424.
FT DOMAIN 57 159 CH.
FT DOMAIN 236 306 EB1 C-terminal.
FT REGION 187 327 DCTN1-binding.
FT REGION 259 302 APC-binding.
FT MOD_RES 167 167 Phosphotyrosine.
FT MOD_RES 219 219 Phosphoserine.
FT VAR_SEQ 1 83 MPGPTQTLSPNGENNNDIIQDNNGTIIPFRKHTVRGERSYS
FT WGMAVNVYSTSITQETMSRHDIIAWVNDIVSLNYTKVEQLC
FT S -> MARTTTTSSRIITGPSFLSGSTQCAGSVPT (in
FT isoform 4).
FT /FTId=VSP_046041.
FT VAR_SEQ 1 40 MPGPTQTLSPNGENNNDIIQDNNGTIIPFRKHTVRGERSY
FT -> MKQNRDQKCPVSQRNSSFQQPGRKPGCS (in
FT isoform 3).
FT /FTId=VSP_045710.
FT VAR_SEQ 252 259 HSLKLALE -> MHQLWPRL (in isoform 2).
FT /FTId=VSP_012944.
FT VAR_SEQ 260 327 Missing (in isoform 2).
FT /FTId=VSP_012945.
FT VARIANT 162 162 Y -> C (in dbSNP:rs11538993).
FT /FTId=VAR_050018.
FT CONFLICT 65 65 A -> G (in Ref. 8; BAA83375).
FT CONFLICT 209 209 S -> G (in Ref. 5; BAG52251).
FT CONFLICT 235 235 K -> I (in Ref. 5; BAH11899).
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
//
MIM
605789
*RECORD*
*FIELD* NO
605789
*FIELD* TI
*605789 MICROTUBULE-ASSOCIATED PROTEIN, RP/EB FAMILY, MEMBER 2; MAPRE2
;;ADENOMATOUS POLYPOSIS COLI-BINDING PROTEIN EB2; EB2;;
read moreAPC-BINDING PROTEIN RP1; RP1
*FIELD* TX
DESCRIPTION
EB1 family proteins (e.g., MAPRE1; 603108) interact with cytoplasmic
microtubules in interphase cells, with mitotic spindles, and with the
adenomatous polyposis coli (APC; 611731) tumor suppressor gene. The
functional inactivation of the APC gene product is a key event in
colorectal tumorigenesis.
CLONING
By differential mRNA display of resting and activated T cells, followed
by 5-prime RACE, Renner et al. (1997) isolated a cDNA encoding MAPRE2,
which they termed RP1. The deduced 327-amino acid protein has
significant homology with EB1 family proteins. Northern blot analysis
detected a 2.6-kb transcript in T cells activated by 2 signals (i.e.,
cell surface antigen(s) and/or cytokine) and also in lymphocyte tumor
cell lines. Immunoprecipitation analysis indicated that RP1 associates
with full-length but not C terminus-deleted APC. Renner et al. (1997)
concluded that RP1 may be an immediate-early T-cell regulatory gene.
Using immunoprecipitation analysis, Juwana et al. (1999) showed that the
N terminus of RP1 interacted with monomeric or polymerized tubulin in
fibrosarcoma cell lines. Immunofluorescence microscopy demonstrated that
RP1 is localized in the plus ends of microtubule networks in the
presence or absence of APC.
GENE STRUCTURE
By genomic sequence analysis, Su and Qi (2001) showed that there are
most likely 3 MAPRE genes: MAPRE1 encodes EB1; MAPRE2 encodes RP1 and
the EB2 fragment; and MAPRE3 (605788) encodes EBF3 and the fragment RP3.
MAPRE2, like MAPRE1 and MAPRE3, contains 7 exons. The coding region of
MAPRE2 spans at least 22 kb.
MAPPING
By radiation hybrid and sequence analyses, Su and Qi (2001) mapped the
MAPRE2 gene to 18q12. By FISH, Wadle et al. (2001) assigned the gene to
18q21.
*FIELD* RF
1. Juwana, J.-P.; Henderikx, P.; Mischo, A.; Wadle, A.; Fadle, N.;
Gerlach, K.; Arends, J. W.; Hoogenboom, H.; Pfreundschuh, M.; Renner,
C.: EB/RP gene family encodes tubulin binding proteins. Int. J.
Cancer 81: 275-284, 1999.
2. Renner, C.; Pfitzenmeier, J.-P.; Gerlach, K.; Held, G.; Ohnesorge,
S.; Sahin, U.; Bauer, S.; Pfreundschuh, M.: RP1, a new member of
the adenomatous polyposis coli-binding EB1-like gene family, is differently
expressed in activated T cells. J. Immun. 159: 1276-1283, 1997.
3. Su, L.-K.; Qi, Y.: Characterization of human MAPRE genes and their
proteins. Genomics 71: 143-149, 2001.
4. Wadle, A.; Thiel, G.; Mischo, A.; Jung, V.; Pfreundschuh, M.; Renner,
C.: Chromosomal localization and promoter analysis of the adenomatous
polyposis coli binding protein RP1. Oncogene 20: 5920-5929, 2001.
*FIELD* CN
Victor A. McKusick - updated: 11/7/2001
*FIELD* CD
Paul J. Converse: 3/28/2001
*FIELD* ED
ckniffin: 02/05/2008
carol: 11/12/2001
terry: 11/7/2001
mgross: 3/29/2001
mgross: 3/28/2001
*RECORD*
*FIELD* NO
605789
*FIELD* TI
*605789 MICROTUBULE-ASSOCIATED PROTEIN, RP/EB FAMILY, MEMBER 2; MAPRE2
;;ADENOMATOUS POLYPOSIS COLI-BINDING PROTEIN EB2; EB2;;
read moreAPC-BINDING PROTEIN RP1; RP1
*FIELD* TX
DESCRIPTION
EB1 family proteins (e.g., MAPRE1; 603108) interact with cytoplasmic
microtubules in interphase cells, with mitotic spindles, and with the
adenomatous polyposis coli (APC; 611731) tumor suppressor gene. The
functional inactivation of the APC gene product is a key event in
colorectal tumorigenesis.
CLONING
By differential mRNA display of resting and activated T cells, followed
by 5-prime RACE, Renner et al. (1997) isolated a cDNA encoding MAPRE2,
which they termed RP1. The deduced 327-amino acid protein has
significant homology with EB1 family proteins. Northern blot analysis
detected a 2.6-kb transcript in T cells activated by 2 signals (i.e.,
cell surface antigen(s) and/or cytokine) and also in lymphocyte tumor
cell lines. Immunoprecipitation analysis indicated that RP1 associates
with full-length but not C terminus-deleted APC. Renner et al. (1997)
concluded that RP1 may be an immediate-early T-cell regulatory gene.
Using immunoprecipitation analysis, Juwana et al. (1999) showed that the
N terminus of RP1 interacted with monomeric or polymerized tubulin in
fibrosarcoma cell lines. Immunofluorescence microscopy demonstrated that
RP1 is localized in the plus ends of microtubule networks in the
presence or absence of APC.
GENE STRUCTURE
By genomic sequence analysis, Su and Qi (2001) showed that there are
most likely 3 MAPRE genes: MAPRE1 encodes EB1; MAPRE2 encodes RP1 and
the EB2 fragment; and MAPRE3 (605788) encodes EBF3 and the fragment RP3.
MAPRE2, like MAPRE1 and MAPRE3, contains 7 exons. The coding region of
MAPRE2 spans at least 22 kb.
MAPPING
By radiation hybrid and sequence analyses, Su and Qi (2001) mapped the
MAPRE2 gene to 18q12. By FISH, Wadle et al. (2001) assigned the gene to
18q21.
*FIELD* RF
1. Juwana, J.-P.; Henderikx, P.; Mischo, A.; Wadle, A.; Fadle, N.;
Gerlach, K.; Arends, J. W.; Hoogenboom, H.; Pfreundschuh, M.; Renner,
C.: EB/RP gene family encodes tubulin binding proteins. Int. J.
Cancer 81: 275-284, 1999.
2. Renner, C.; Pfitzenmeier, J.-P.; Gerlach, K.; Held, G.; Ohnesorge,
S.; Sahin, U.; Bauer, S.; Pfreundschuh, M.: RP1, a new member of
the adenomatous polyposis coli-binding EB1-like gene family, is differently
expressed in activated T cells. J. Immun. 159: 1276-1283, 1997.
3. Su, L.-K.; Qi, Y.: Characterization of human MAPRE genes and their
proteins. Genomics 71: 143-149, 2001.
4. Wadle, A.; Thiel, G.; Mischo, A.; Jung, V.; Pfreundschuh, M.; Renner,
C.: Chromosomal localization and promoter analysis of the adenomatous
polyposis coli binding protein RP1. Oncogene 20: 5920-5929, 2001.
*FIELD* CN
Victor A. McKusick - updated: 11/7/2001
*FIELD* CD
Paul J. Converse: 3/28/2001
*FIELD* ED
ckniffin: 02/05/2008
carol: 11/12/2001
terry: 11/7/2001
mgross: 3/29/2001
mgross: 3/28/2001