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Q9UPY8

- MARE3_HUMAN

UniProt

Q9UPY8 - MARE3_HUMAN

Protein

Microtubule-associated protein RP/EB family member 3

Gene

MAPRE3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration By similarity.By similarity

    GO - Molecular functioni

    1. microtubule binding Source: BHF-UCL
    2. protein binding Source: BHF-UCL

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB-KW
    2. positive regulation of cyclin-dependent protein serine/threonine kinase activity Source: BHF-UCL
    3. positive regulation of transcription, DNA-templated Source: BHF-UCL

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microtubule-associated protein RP/EB family member 3
    Alternative name(s):
    EB1 protein family member 3
    Short name:
    EBF3
    End-binding protein 3
    Short name:
    EB3
    RP3
    Gene namesi
    Name:MAPRE3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6892. MAPRE3.

    Subcellular locationi

    Cytoplasmcytoskeleton 2 Publications
    Note: Associated with the microtubule network. Detected at the plus end of microtubules.

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. microtubule Source: UniProtKB-KW
    3. microtubule cytoskeleton Source: BHF-UCL
    4. midbody Source: BHF-UCL
    5. perinuclear region of cytoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30636.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 281281Microtubule-associated protein RP/EB family member 3PRO_0000213428Add
    BLAST

    Proteomic databases

    MaxQBiQ9UPY8.
    PaxDbiQ9UPY8.
    PRIDEiQ9UPY8.

    PTM databases

    PhosphoSiteiQ9UPY8.

    Expressioni

    Tissue specificityi

    Predominantly expressed in brain and muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ9UPY8.
    BgeeiQ9UPY8.
    CleanExiHS_MAPRE3.
    GenevestigatoriQ9UPY8.

    Organism-specific databases

    HPAiHPA009263.

    Interactioni

    Subunit structurei

    Interacts with APC2 By similarity. Homodimer. Heterodimer with MAPRE1. Interacts with DCTN1 and SRCIN1. Binds to the C-terminal domain of APC. Binds monomeric and polymerized tubulin. Interacts (via C-terminus) with CLIP1. Interacts with SLAIN2.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APC2O959967EBI-726739,EBI-1053045
    JUNP054123EBI-726739,EBI-852823
    Srcin1Q9QWI6-25EBI-726739,EBI-775607From a different organism.

    Protein-protein interaction databases

    BioGridi116584. 8 interactions.
    DIPiDIP-56069N.
    IntActiQ9UPY8. 12 interactions.
    MINTiMINT-1417856.
    STRINGi9606.ENSP00000233121.

    Structurei

    Secondary structure

    1
    281
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 2812
    Helixi35 – 406
    Helixi42 – 5110
    Helixi58 – 603
    Helixi68 – 8518
    Helixi93 – 975
    Helixi101 – 11818
    Turni126 – 1294
    Helixi206 – 23833
    Helixi247 – 2559

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WYONMR-A1-146[»]
    3CO1X-ray1.40A1-130[»]
    3TQ7X-ray2.30B200-281[»]
    ProteinModelPortaliQ9UPY8.
    SMRiQ9UPY8. Positions 1-147, 204-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UPY8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 116103CHPROSITE-ProRule annotationAdd
    BLAST
    Domaini194 – 26471EB1 C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni217 – 28165DCTN1-bindingAdd
    BLAST
    Regioni217 – 26044APC-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.
    InParanoidiQ9UPY8.
    KOiK10436.
    OMAiNYHALER.
    OrthoDBiEOG7ZD1W5.
    PhylomeDBiQ9UPY8.
    TreeFamiTF313620.

    Family and domain databases

    Gene3Di1.10.418.10. 1 hit.
    InterProiIPR001715. CH-domain.
    IPR004953. EB1_C.
    IPR027738. EB3_vertebrate.
    IPR027328. MAPRE.
    [Graphical view]
    PANTHERiPTHR10623. PTHR10623. 1 hit.
    PTHR10623:SF10. PTHR10623:SF10. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UPY8-1) [UniParc]FASTAAdd to Basket

    Also known as: EBF3-L

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAVNVYSTSV TSENLSRHDM LAWVNDSLHL NYTKIEQLCS GAAYCQFMDM    50
    LFPGCVHLRK VKFQAKLEHE YIHNFKVLQA AFKKMGVDKI IPVEKLVKGK 100
    FQDNFEFIQW FKKFFDANYD GKDYNPLLAR QGQDVAPPPN PGDQIFNKSK 150
    KLIGTAVPQR TSPTGPKNMQ TSGRLSNVAP PCILRKNPPS ARNGGHETDA 200
    QILELNQQLV DLKLTVDGLE KERDFYFSKL RDIELICQEH ESENSPVISG 250
    IIGILYATEE GFAPPEDDEI EEHQQEDQDE Y 281
    Length:281
    Mass (Da):31,982
    Last modified:May 1, 2000 - v1
    Checksum:i0DA45E89A0B993D3
    GO
    Isoform 2 (identifier: Q9UPY8-2) [UniParc]FASTAAdd to Basket

    Also known as: EBF3-S

    The sequence of this isoform differs from the canonical sequence as follows:
         142-156: Missing.

    Show »
    Length:266
    Mass (Da):30,380
    Checksum:iE66CAD36E28EE645
    GO

    Sequence cautioni

    The sequence CAA72060.1 differs from that shown. Reason: Frameshift at position 199.
    The sequence AAK07556.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAK07557.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → P in CAA72060. (PubMed:9233623)Curated
    Sequence conflicti13 – 131E → V in CAA72060. (PubMed:9233623)Curated
    Sequence conflicti123 – 1231D → G in CAA72060. (PubMed:9233623)Curated
    Sequence conflicti237 – 2371C → S in CAG38760. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei142 – 15615Missing in isoform 2. 1 PublicationVSP_012947Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025186 mRNA. Translation: BAA82958.1.
    AF288787 Genomic DNA. Translation: AAK07556.1. Different initiation.
    AF288787 Genomic DNA. Translation: AAK07557.1. Different initiation.
    CR536523 mRNA. Translation: CAG38760.1.
    CR541845 mRNA. Translation: CAG46643.1.
    AC013472 Genomic DNA. Translation: AAY14653.1.
    CH471053 Genomic DNA. Translation: EAX00660.1.
    CH471053 Genomic DNA. Translation: EAX00662.1.
    CH471053 Genomic DNA. Translation: EAX00663.1.
    CH471053 Genomic DNA. Translation: EAX00666.1.
    BC011557 mRNA. Translation: AAH11557.1.
    Y11174 mRNA. Translation: CAA72060.1. Frameshift.
    CCDSiCCDS1731.1. [Q9UPY8-1]
    RefSeqiNP_036458.2. NM_012326.2. [Q9UPY8-1]
    XP_006712030.1. XM_006711967.1. [Q9UPY8-2]
    UniGeneiHs.515860.

    Genome annotation databases

    EnsembliENST00000233121; ENSP00000233121; ENSG00000084764. [Q9UPY8-1]
    ENST00000402218; ENSP00000385715; ENSG00000084764. [Q9UPY8-2]
    ENST00000405074; ENSP00000383915; ENSG00000084764. [Q9UPY8-2]
    GeneIDi22924.
    KEGGihsa:22924.
    UCSCiuc002rhw.3. human. [Q9UPY8-1]

    Polymorphism databases

    DMDMi20138791.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025186 mRNA. Translation: BAA82958.1 .
    AF288787 Genomic DNA. Translation: AAK07556.1 . Different initiation.
    AF288787 Genomic DNA. Translation: AAK07557.1 . Different initiation.
    CR536523 mRNA. Translation: CAG38760.1 .
    CR541845 mRNA. Translation: CAG46643.1 .
    AC013472 Genomic DNA. Translation: AAY14653.1 .
    CH471053 Genomic DNA. Translation: EAX00660.1 .
    CH471053 Genomic DNA. Translation: EAX00662.1 .
    CH471053 Genomic DNA. Translation: EAX00663.1 .
    CH471053 Genomic DNA. Translation: EAX00666.1 .
    BC011557 mRNA. Translation: AAH11557.1 .
    Y11174 mRNA. Translation: CAA72060.1 . Frameshift.
    CCDSi CCDS1731.1. [Q9UPY8-1 ]
    RefSeqi NP_036458.2. NM_012326.2. [Q9UPY8-1 ]
    XP_006712030.1. XM_006711967.1. [Q9UPY8-2 ]
    UniGenei Hs.515860.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WYO NMR - A 1-146 [» ]
    3CO1 X-ray 1.40 A 1-130 [» ]
    3TQ7 X-ray 2.30 B 200-281 [» ]
    ProteinModelPortali Q9UPY8.
    SMRi Q9UPY8. Positions 1-147, 204-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116584. 8 interactions.
    DIPi DIP-56069N.
    IntActi Q9UPY8. 12 interactions.
    MINTi MINT-1417856.
    STRINGi 9606.ENSP00000233121.

    PTM databases

    PhosphoSitei Q9UPY8.

    Polymorphism databases

    DMDMi 20138791.

    Proteomic databases

    MaxQBi Q9UPY8.
    PaxDbi Q9UPY8.
    PRIDEi Q9UPY8.

    Protocols and materials databases

    DNASUi 22924.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233121 ; ENSP00000233121 ; ENSG00000084764 . [Q9UPY8-1 ]
    ENST00000402218 ; ENSP00000385715 ; ENSG00000084764 . [Q9UPY8-2 ]
    ENST00000405074 ; ENSP00000383915 ; ENSG00000084764 . [Q9UPY8-2 ]
    GeneIDi 22924.
    KEGGi hsa:22924.
    UCSCi uc002rhw.3. human. [Q9UPY8-1 ]

    Organism-specific databases

    CTDi 22924.
    GeneCardsi GC02P027193.
    HGNCi HGNC:6892. MAPRE3.
    HPAi HPA009263.
    MIMi 605788. gene.
    neXtProti NX_Q9UPY8.
    PharmGKBi PA30636.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5217.
    HOGENOMi HOG000198048.
    HOVERGENi HBG052410.
    InParanoidi Q9UPY8.
    KOi K10436.
    OMAi NYHALER.
    OrthoDBi EOG7ZD1W5.
    PhylomeDBi Q9UPY8.
    TreeFami TF313620.

    Miscellaneous databases

    EvolutionaryTracei Q9UPY8.
    GeneWikii MAPRE3.
    GenomeRNAii 22924.
    NextBioi 43629.
    PROi Q9UPY8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UPY8.
    Bgeei Q9UPY8.
    CleanExi HS_MAPRE3.
    Genevestigatori Q9UPY8.

    Family and domain databases

    Gene3Di 1.10.418.10. 1 hit.
    InterProi IPR001715. CH-domain.
    IPR004953. EB1_C.
    IPR027738. EB3_vertebrate.
    IPR027328. MAPRE.
    [Graphical view ]
    PANTHERi PTHR10623. PTHR10623. 1 hit.
    PTHR10623:SF10. PTHR10623:SF10. 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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH APC2, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Fetal brain.
    2. "Characterization of human MAPRE genes and their proteins."
      Su L.-K., Qi Y.
      Genomics 71:142-149(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Kidney.
    7. "RP1, a new member of the adenomatous polyposis coli-binding EB1-like gene family, is differentially expressed in activated T cells."
      Renner C., Pfitzenmeier J.-P., Gerlach K., Held G., Ohnesorge S., Sahin U., Bauer S., Pfreundschuh M.
      J. Immunol. 159:1276-1283(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-200 (ISOFORM 1).
    8. Cited for: INTERACTION WITH TUBULIN.
    9. "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.
    10. "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.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: INTERACTION WITH SRCIN1.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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.
    15. "Solution structure of the CH domain of human microtubule-associated protein RP/EB family member 3."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-146.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-130, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiMARE3_HUMAN
    AccessioniPrimary (citable) accession number: Q9UPY8
    Secondary accession number(s): B7WPK5
    , O00265, Q6FHB0, Q6FI15, Q9BZP7, Q9BZP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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