Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15691

- MARE1_HUMAN

UniProt

Q15691 - MARE1_HUMAN

Protein

Microtubule-associated protein RP/EB family member 1

Gene

MAPRE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.4 Publications

    GO - Molecular functioni

    1. microtubule plus-end binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein C-terminus binding Source: ProtInc

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. G2/M transition of mitotic cell cycle Source: Reactome
    3. mitotic cell cycle Source: Reactome
    4. mitotic nuclear division Source: UniProtKB-KW
    5. negative regulation of microtubule polymerization Source: UniProtKB
    6. protein localization to microtubule Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microtubule-associated protein RP/EB family member 1
    Alternative name(s):
    APC-binding protein EB1
    End-binding protein 1
    Short name:
    EB1
    Gene namesi
    Name:MAPRE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:6890. MAPRE1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    Note: Associated with the microtubule network at the growing distal tip of microtubules. Also enriched at the centrosome.

    GO - Cellular componenti

    1. cell projection membrane Source: Ensembl
    2. centrosome Source: UniProtKB
    3. cortical microtubule cytoskeleton Source: UniProtKB
    4. cytoplasm Source: HPA
    5. cytoplasmic microtubule Source: Ensembl
    6. cytosol Source: Reactome
    7. Golgi apparatus Source: Ensembl
    8. microtubule Source: UniProtKB
    9. microtubule plus-end Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi59 – 602KK → EE: No effect.
    Mutagenesisi89 – 891K → E: Loss of binding to microtubules. 1 Publication

    Organism-specific databases

    PharmGKBiPA30634.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 268267Microtubule-associated protein RP/EB family member 1PRO_0000213416Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei124 – 1241Phosphotyrosine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15691.
    PaxDbiQ15691.
    PeptideAtlasiQ15691.
    PRIDEiQ15691.

    2D gel databases

    OGPiQ15691.
    REPRODUCTION-2DPAGEIPI00017596.

    PTM databases

    PhosphoSiteiQ15691.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    BgeeiQ15691.
    CleanExiHS_MAPRE1.
    GenevestigatoriQ15691.

    Organism-specific databases

    HPAiCAB009337.
    CAB019391.
    HPA003600.

    Interactioni

    Subunit structurei

    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.By similarity19 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APCP250544EBI-1004115,EBI-727707
    APC2O959963EBI-1004115,EBI-1053045
    DSTQ030012EBI-1004115,EBI-310758
    KIF2CQ996615EBI-1004115,EBI-1642317
    MTUS2Q5JR597EBI-1004115,EBI-742948
    TERF1P542742EBI-1004115,EBI-710997

    Protein-protein interaction databases

    BioGridi116581. 34 interactions.
    DIPiDIP-38018N.
    IntActiQ15691. 19 interactions.
    MINTiMINT-206298.
    STRINGi9606.ENSP00000364721.

    Structurei

    Secondary structure

    1
    268
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 2812
    Helixi35 – 406
    Helixi42 – 5110
    Helixi58 – 603
    Helixi68 – 8518
    Helixi93 – 964
    Turni97 – 993
    Helixi101 – 11818
    Helixi126 – 1294
    Helixi192 – 23039
    Turni231 – 2333
    Helixi237 – 24711
    Beta strandi250 – 2523

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ15691.
    SMRiQ15691. Positions 1-132, 191-257.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15691.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 116103CHPROSITE-ProRule annotationAdd
    BLAST
    Domaini185 – 25571EB1 C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni124 – 268145Interaction with MTUS2/TIP150Add
    BLAST
    Regioni185 – 26884Interaction with CDK5RAP2Add
    BLAST
    Regioni208 – 26861DCTN1-bindingAdd
    BLAST
    Regioni220 – 24223APC-bindingAdd
    BLAST

    Domaini

    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 similaritiesi

    Belongs to the MAPRE family.Curated
    Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
    Contains 1 EB1 C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5217.
    HOGENOMiHOG000198048.
    HOVERGENiHBG052410.
    InParanoidiQ15691.
    KOiK10436.
    OMAiATPPNRM.
    OrthoDBiEOG7ZD1W5.
    PhylomeDBiQ15691.
    TreeFamiTF313620.

    Family and domain databases

    Gene3Di1.10.418.10. 1 hit.
    InterProiIPR001715. CH-domain.
    IPR004953. EB1_C.
    IPR027739. EB1_vertebrate.
    IPR027328. MAPRE.
    [Graphical view]
    PANTHERiPTHR10623. PTHR10623. 1 hit.
    PTHR10623:SF13. PTHR10623:SF13. 1 hit.
    PfamiPF00307. CH. 1 hit.
    PF03271. EB1. 1 hit.
    [Graphical view]
    SUPFAMiSSF140612. SSF140612. 1 hit.
    SSF47576. SSF47576. 1 hit.
    PROSITEiPS50021. CH. 1 hit.
    PS51230. EB1_C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q15691-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GAAYCQFMDM    50
    LFPGSIALKK VKFQAKLEHE YIQNFKILQA GFKRMGVDKI IPVDKLVKGK 100
    FQDNFEFVQW FKKFFDANYD GKDYDPVAAR QGQETAVAPS LVAPALNKPK 150
    KPLTSSSAAP QRPISTQRTA AAPKAGPGVV RKNPGVGNGD DEAAELMQQV 200
    NVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ RIVDILYATD 250
    EGFVIPDEGG PQEEQEEY 268
    Length:268
    Mass (Da):29,999
    Last modified:January 23, 2007 - v3
    Checksum:i08C8999F45A145ED
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13208.1.
    PIRiI52726.
    RefSeqiNP_036457.1. NM_012325.2.
    UniGeneiHs.472437.

    Genome annotation databases

    EnsembliENST00000375571; ENSP00000364721; ENSG00000101367.
    GeneIDi22919.
    KEGGihsa:22919.
    UCSCiuc002wyh.3. human.

    Polymorphism databases

    DMDMi20138589.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS13208.1.
    PIRi I52726.
    RefSeqi NP_036457.1. NM_012325.2.
    UniGenei Hs.472437.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PA7 X-ray 1.45 A 1-130 [» ]
    1TXQ X-ray 1.80 B 183-268 [» ]
    1UEG X-ray 2.40 A 1-130 [» ]
    1VKA X-ray 1.60 A/B 2-140 [» ]
    1WU9 X-ray 1.54 A/B 191-268 [» ]
    1YIB X-ray 1.80 A 185-255 [» ]
    1YIG X-ray 2.00 A/B 185-255 [» ]
    2HKQ X-ray 1.86 A 191-268 [» ]
    2HL3 X-ray 2.03 C 263-268 [» ]
    2HL5 X-ray 1.93 A/B 191-268 [» ]
    2QJZ X-ray 1.25 A/B 12-133 [» ]
    2R8U X-ray 1.35 A/B 1-268 [» ]
    3GJO X-ray 2.50 A/B/C/D 191-260 [» ]
    3MTU X-ray 2.10 A/B/C/D 215-257 [» ]
    3TQ7 X-ray 2.30 A 191-268 [» ]
    ProteinModelPortali Q15691.
    SMRi Q15691. Positions 1-132, 191-257.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116581. 34 interactions.
    DIPi DIP-38018N.
    IntActi Q15691. 19 interactions.
    MINTi MINT-206298.
    STRINGi 9606.ENSP00000364721.

    PTM databases

    PhosphoSitei Q15691.

    Polymorphism databases

    DMDMi 20138589.

    2D gel databases

    OGPi Q15691.
    REPRODUCTION-2DPAGE IPI00017596.

    Proteomic databases

    MaxQBi Q15691.
    PaxDbi Q15691.
    PeptideAtlasi Q15691.
    PRIDEi Q15691.

    Protocols and materials databases

    DNASUi 22919.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375571 ; ENSP00000364721 ; ENSG00000101367 .
    GeneIDi 22919.
    KEGGi hsa:22919.
    UCSCi uc002wyh.3. human.

    Organism-specific databases

    CTDi 22919.
    GeneCardsi GC20P031407.
    HGNCi HGNC:6890. MAPRE1.
    HPAi CAB009337.
    CAB019391.
    HPA003600.
    MIMi 603108. gene.
    neXtProti NX_Q15691.
    PharmGKBi PA30634.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5217.
    HOGENOMi HOG000198048.
    HOVERGENi HBG052410.
    InParanoidi Q15691.
    KOi K10436.
    OMAi ATPPNRM.
    OrthoDBi EOG7ZD1W5.
    PhylomeDBi Q15691.
    TreeFami TF313620.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    ChiTaRSi MAPRE1. human.
    EvolutionaryTracei Q15691.
    GeneWikii MAPRE1.
    GenomeRNAii 22919.
    NextBioi 43617.
    PROi Q15691.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15691.
    CleanExi HS_MAPRE1.
    Genevestigatori Q15691.

    Family and domain databases

    Gene3Di 1.10.418.10. 1 hit.
    InterProi IPR001715. CH-domain.
    IPR004953. EB1_C.
    IPR027739. EB1_vertebrate.
    IPR027328. MAPRE.
    [Graphical view ]
    PANTHERi PTHR10623. PTHR10623. 1 hit.
    PTHR10623:SF13. PTHR10623:SF13. 1 hit.
    Pfami PF00307. CH. 1 hit.
    PF03271. EB1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF140612. SSF140612. 1 hit.
    SSF47576. SSF47576. 1 hit.
    PROSITEi PS50021. CH. 1 hit.
    PS51230. EB1_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. 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. 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiMARE1_HUMAN
    AccessioniPrimary (citable) accession number: Q15691
    Secondary accession number(s): B2R6I7, E1P5M8, Q3KQS8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 154 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3