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Q15691 (MARE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated protein RP/EB family member 1
Alternative name(s):
APC-binding protein EB1
End-binding protein 1
Short name=EB1
Gene names
Name:MAPRE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration. Ref.12 Ref.23 Ref.29 Ref.32

Subunit structure

Homodimer. Heterodimer with MAPRE3. Interacts with DCTN1, DCTN2, DIAPH1, DIAPH2, TERF1 and dynein intermediate chain. Interacts with APC (via C-terminal domain), CLASP2, DST, KIF2C and STIM1; probably required for their targeting to the growing microtubule plus ends. Interacts with MTUS2; interaction is direct and probably targets MTUS2 to microtubules. Interacts with APC2. Interacts with CLASP1. Interacts with CDK5RAP2. Interacts with MACF1 By similarity. Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 By similarity. Interacts (via C-terminus) with CLIP1. Interacts with SLAIN2. Interacts with KIF18B; this interaction is required for efficient accumulation of KIF18B at microtubule plus ends. Interacts with MISP. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.26 Ref.27 Ref.29 Ref.32

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Associated with the microtubule network at the growing distal tip of microtubules. Also enriched at the centrosome. Ref.7 Ref.12 Ref.23 Ref.29 Ref.32

Tissue specificity

Ubiquitously expressed. Ref.10

Domain

Composed of two functionally independent domains. The N-terminal domain forms a hydrophobic cleft involved in microtubule binding and the C-terminal is involved in the formation of mutually exclusive complexes with APC and DCTN1.

Sequence similarities

Belongs to the MAPRE family.

Contains 1 CH (calponin-homology) domain.

Contains 1 EB1 C-terminal domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of microtubule polymerization

Inferred from direct assay Ref.11. Source: UniProtKB

protein localization to microtubule

Inferred from direct assay Ref.32. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cell projection membrane

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cortical microtubule cytoskeleton

Inferred from direct assay Ref.14. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic microtubule

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

microtubule

Inferred from direct assay PubMed 10773885. Source: UniProtKB

microtubule plus-end

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmicrotubule plus-end binding

Inferred from direct assay Ref.14Ref.32. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein C-terminus binding

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction Ref.8PubMed 10773885Ref.11Ref.14Ref.18Ref.20Ref.32Ref.23. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 268267Microtubule-associated protein RP/EB family member 1
PRO_0000213416

Regions

Domain14 – 116103CH
Domain185 – 25571EB1 C-terminal
Region124 – 268145Interaction with MTUS2/TIP150
Region185 – 26884Interaction with CDK5RAP2
Region208 – 26861DCTN1-binding
Region220 – 24223APC-binding

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.17 Ref.24 Ref.25
Modified residue1241Phosphotyrosine Ref.15

Experimental info

Mutagenesis59 – 602KK → EE: No effect.
Mutagenesis891K → E: Loss of binding to microtubules. Ref.28

Secondary structure

......................... 268
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15691 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 08C8999F45A145ED

FASTA26829,999
        10         20         30         40         50         60 
MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GAAYCQFMDM LFPGSIALKK 

        70         80         90        100        110        120 
VKFQAKLEHE YIQNFKILQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD 

       130        140        150        160        170        180 
GKDYDPVAAR QGQETAVAPS LVAPALNKPK KPLTSSSAAP QRPISTQRTA AAPKAGPGVV 

       190        200        210        220        230        240 
RKNPGVGNGD DEAAELMQQV NVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ 

       250        260 
RIVDILYATD EGFVIPDEGG PQEEQEEY 

« Hide

References

« Hide 'large scale' references
[1]"APC binds to the novel protein EB1."
Su L.-K., Burrell M., Hill D.E., Gyuris J., Brent R., Wiltshire R., Trent J., Vogelstein B., Kinzler K.W.
Cancer Res. 55:2972-2977(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH APC.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]Bienvenut W.V., Potts A., Barblan J., Quadroni M.
Submitted (JUL-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-17, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[7]"The adenomatous polyposis coli-binding protein EB1 is associated with cytoplasmic and spindle microtubules."
Berrueta L., Kraeft S.-K., Tirnauer J.S., Schuyler S.C., Chen L.B., Hill D.E., Pellman D., Bierer B.E.
Proc. Natl. Acad. Sci. U.S.A. 95:10596-10601(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain."
Berrueta L., Tirnauer J.S., Schuyler S.C., Pellman D., Bierer B.E.
Curr. Biol. 9:425-428(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCTN1; DCTN2 AND DYNEIN INTERMEDIATE CHAIN.
[9]"EB/RP gene family encodes tubulin binding proteins."
Juwana J.-P., Henderikx P., Mischo A., Wadle A., Fadle N., Gerlach K., Arends J.W., Hoogenboom H., Pfreundschuh M., Renner C.
Int. J. Cancer 81:275-284(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TUBULIN.
[10]"EB3, a novel member of the EB1 family preferentially expressed in the central nervous system, binds to a CNS-specific APC homologue."
Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.
Oncogene 19:210-216(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APC2, TISSUE SPECIFICITY.
[11]"Involvement of the telomeric protein Pin2/TRF1 in the regulation of the mitotic spindle."
Nakamura M., Zhen Zhou X., Kishi S., Ping Lu K.
FEBS Lett. 514:193-198(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TERF1.
[12]"Evidence that an interaction between EB1 and p150(Glued) is required for the formation and maintenance of a radial microtubule array anchored at the centrosome."
Askham J.M., Vaughan K.T., Goodson H.V., Morrison E.E.
Mol. Biol. Cell 13:3627-3645(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APC AND DCTN1, SUBCELLULAR LOCATION, FUNCTION.
[13]"Characterization of functional domains of human EB1 family proteins."
Bu W., Su L.-K.
J. Biol. Chem. 278:49721-49731(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, INTERACTION WITH TUBULIN; APC AND DCTN1.
[14]"CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics at the cell cortex."
Mimori-Kiyosue Y., Grigoriev I., Lansbergen G., Sasaki H., Matsui C., Severin F., Galjart N., Grosveld F., Vorobjev I., Tsukita S., Akhmanova A.
J. Cell Biol. 168:141-153(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLASP1 AND CLASP2.
[15]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition."
Mishima M., Maesaki R., Kasa M., Watanabe T., Fukata M., Kaibuchi K., Hakoshima T.
Proc. Natl. Acad. Sci. U.S.A. 104:10346-10351(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLIP1.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"TIP150 interacts with and targets MCAK at the microtubule plus ends."
Jiang K., Wang J., Liu J., Ward T., Wordeman L., Davidson A., Wang F., Yao X.
EMBO Rep. 10:857-865(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MTUS2 AND KIF2C.
[19]"Mammalian end binding proteins control persistent microtubule growth."
Komarova Y., De Groot C.O., Grigoriev I., Gouveia S.M., Munteanu E.L., Schober J.M., Honnappa S., Buey R.M., Hoogenraad C.C., Dogterom M., Borisy G.G., Steinmetz M.O., Akhmanova A.
J. Cell Biol. 184:691-706(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPRE3.
[20]"Interaction of CDK5RAP2 with EB1 to track growing microtubule tips and to regulate microtubule dynamics."
Fong K.W., Hau S.Y., Kho Y.S., Jia Y., He L., Qi R.Z.
Mol. Biol. Cell 20:3660-3670(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK5RAP2.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"A complex of Kif18b and MCAK promotes microtubule depolymerization and is negatively regulated by Aurora kinases."
Tanenbaum M.E., Macurek L., van der Vaart B., Galli M., Akhmanova A., Medema R.H.
Curr. Biol. 21:1356-1365(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIF18B.
[23]"SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase."
van der Vaart B., Manatschal C., Grigoriev I., Olieric V., Gouveia S.M., Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C., Steinmetz M.O., Akhmanova A.
J. Cell Biol. 193:1083-1099(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLAIN2 AND CLIP1, FUNCTION, SUBCELLULAR LOCATION.
[24]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"MISP is a novel Plk1 substrate required for proper spindle orientation and mitotic progression."
Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P., Goenczy P., Hoffmann I.
J. Cell Biol. 200:773-787(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MISP.
[27]"Structural insights into the EB1-APC interaction."
Honnappa S., John C.M., Kostrewa D., Winkler F.K., Steinmetz M.O.
EMBO J. 24:261-269(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 191-268, DIMERIZATION, INTERACTION WITH APC.
[28]"Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)."
Hayashi I., Ikura M.
J. Biol. Chem. 278:36430-36434(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-130, MUTAGENESIS OF 59-LYS-LYS-60 AND LYS-89.
[29]"Structural basis for the activation of microtubule assembly by the EB1 and p150Glued complex."
Hayashi I., Wilde A., Mal T.K., Ikura M.
Mol. Cell 19:449-460(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 183-268 IN COMPLEX WITH DCTN1, FUNCTION, SUBUNIT, INTERACTION WITH DCTN1, SUBCELLULAR LOCATION.
[30]"Key interaction modes of dynamic +TIP networks."
Honnappa S., Okhrimenko O., Jaussi R., Jawhari H., Jelesarov I., Winkler F.K., Steinmetz M.O.
Mol. Cell 23:663-671(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 191-267 IN COMPLEX WITH DCTN1.
[31]"Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1."
Slep K.C., Vale R.D.
Mol. Cell 27:976-991(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 12-133.
[32]"An EB1-binding motif acts as a microtubule tip localization signal."
Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S., Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A., Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.
Cell 138:366-376(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 191-260 IN COMPLEX WITH DST, FUNCTION, INTERACTION WITH APC; CLASP2; KIF2C AND STIM1, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U24166 mRNA. Translation: AAC09471.1.
AK312590 mRNA. Translation: BAG35484.1.
AL035071 Genomic DNA. Translation: CAB53072.1.
CH471077 Genomic DNA. Translation: EAW76348.1.
CH471077 Genomic DNA. Translation: EAW76349.1.
BC106068 mRNA. Translation: AAI06069.1.
BC109281 mRNA. Translation: AAI09282.1.
CCDSCCDS13208.1.
PIRI52726.
RefSeqNP_036457.1. NM_012325.2.
UniGeneHs.472437.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PA7X-ray1.45A1-130[»]
1TXQX-ray1.80B183-268[»]
1UEGX-ray2.40A1-130[»]
1VKAX-ray1.60A/B2-140[»]
1WU9X-ray1.54A/B191-268[»]
1YIBX-ray1.80A185-255[»]
1YIGX-ray2.00A/B185-255[»]
2HKQX-ray1.86A191-268[»]
2HL3X-ray2.03C263-268[»]
2HL5X-ray1.93A/B191-268[»]
2QJZX-ray1.25A/B12-133[»]
2R8UX-ray1.35A/B1-268[»]
3GJOX-ray2.50A/B/C/D191-260[»]
3MTUX-ray2.10A/B/C/D215-257[»]
3TQ7X-ray2.30A191-268[»]
ProteinModelPortalQ15691.
SMRQ15691. Positions 1-132, 191-257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116581. 34 interactions.
DIPDIP-38018N.
IntActQ15691. 19 interactions.
MINTMINT-206298.
STRING9606.ENSP00000364721.

PTM databases

PhosphoSiteQ15691.

Polymorphism databases

DMDM20138589.

2D gel databases

OGPQ15691.
REPRODUCTION-2DPAGEIPI00017596.

Proteomic databases

MaxQBQ15691.
PaxDbQ15691.
PeptideAtlasQ15691.
PRIDEQ15691.

Protocols and materials databases

DNASU22919.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375571; ENSP00000364721; ENSG00000101367.
GeneID22919.
KEGGhsa:22919.
UCSCuc002wyh.3. human.

Organism-specific databases

CTD22919.
GeneCardsGC20P031407.
HGNCHGNC:6890. MAPRE1.
HPACAB009337.
CAB019391.
HPA003600.
MIM603108. gene.
neXtProtNX_Q15691.
PharmGKBPA30634.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5217.
HOGENOMHOG000198048.
HOVERGENHBG052410.
InParanoidQ15691.
KOK10436.
OMAATPPNRM.
OrthoDBEOG7ZD1W5.
PhylomeDBQ15691.
TreeFamTF313620.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

BgeeQ15691.
CleanExHS_MAPRE1.
GenevestigatorQ15691.

Family and domain databases

Gene3D1.10.418.10. 1 hit.
InterProIPR001715. CH-domain.
IPR004953. EB1_C.
IPR027739. EB1_vertebrate.
IPR027328. MAPRE.
[Graphical view]
PANTHERPTHR10623. PTHR10623. 1 hit.
PTHR10623:SF13. PTHR10623:SF13. 1 hit.
PfamPF00307. CH. 1 hit.
PF03271. EB1. 1 hit.
[Graphical view]
SUPFAMSSF140612. SSF140612. 1 hit.
SSF47576. SSF47576. 1 hit.
PROSITEPS50021. CH. 1 hit.
PS51230. EB1_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAPRE1. human.
EvolutionaryTraceQ15691.
GeneWikiMAPRE1.
GenomeRNAi22919.
NextBio43617.
PROQ15691.
SOURCESearch...

Entry information

Entry nameMARE1_HUMAN
AccessionPrimary (citable) accession number: Q15691
Secondary accession number(s): B2R6I7, E1P5M8, Q3KQS8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM