MAPRE1

Protein-coding gene in the species Homo sapiens
MAPRE1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1PA7, 1TXQ, 1UEG, 1VKA, 1WU9, 1YIB, 1YIG, 2HKQ, 2HL3, 2HL5, 2QJZ, 2R8U, 3GJO, 3MTU, 3TQ7, 4XA1, 4XA3, 4XA6

Identifiers
AliasesMAPRE1, EB1, microtubule associated protein RP/EB family member 1
External IDsOMIM: 603108 MGI: 891995 HomoloGene: 56129 GeneCards: MAPRE1
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for MAPRE1
Genomic location for MAPRE1
Band20q11.21Start32,819,954 bp[1]
End32,850,405 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for MAPRE1
Genomic location for MAPRE1
Band2 H1|2 75.95 cMStart153,583,194 bp[2]
End153,615,230 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • ganglionic eminence

  • islet of Langerhans

  • monocyte

  • bone marrow

  • pancreatic epithelial cell

  • smooth muscle tissue

  • pancreatic ductal cell

  • appendix

  • visceral pleura
Top expressed in
  • medial ganglionic eminence

  • retinal pigment epithelium

  • dermis

  • atrioventricular valve

  • maxillary prominence

  • atrium

  • endocardial cushion

  • epithelium of stomach

  • molar

  • sciatic nerve
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein binding
  • microtubule binding
  • protein C-terminus binding
  • microtubule plus-end binding
  • identical protein binding
  • RNA binding
  • cadherin binding
  • protein kinase binding
Cellular component
  • microtubule plus-end
  • microtubule cytoskeleton
  • microtubule organizing center
  • cortical microtubule cytoskeleton
  • cell projection membrane
  • Golgi apparatus
  • centrosome
  • cytoskeleton
  • cell projection
  • spindle
  • cytoplasmic microtubule
  • cytosol
  • microtubule
  • cytoplasm
  • focal adhesion
  • spindle midzone
  • mitotic spindle astral microtubule end
Biological process
  • G2/M transition of mitotic cell cycle
  • positive regulation of microtubule plus-end binding
  • cell population proliferation
  • negative regulation of microtubule polymerization
  • cell division
  • cell cycle
  • protein localization to microtubule
  • sister chromatid cohesion
  • negative regulation of microtubule binding
  • positive regulation of cell migration
  • ciliary basal body-plasma membrane docking
  • regulation of microtubule cytoskeleton organization
  • regulation of G2/M transition of mitotic cell cycle
  • protein localization
  • cell migration
  • regulation of microtubule polymerization or depolymerization
  • positive regulation of microtubule polymerization
  • spindle assembly
  • protein localization to microtubule plus-end
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

22919

13589

Ensembl

ENSG00000101367

ENSMUSG00000027479

UniProt

Q15691

Q61166

RefSeq (mRNA)

NM_012325

NM_007896

RefSeq (protein)

NP_036457

NP_031922

Location (UCSC)Chr 20: 32.82 – 32.85 MbChr 2: 153.58 – 153.62 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Microtubule-associated protein RP/EB family member 1 is a protein that in humans is encoded by the MAPRE1 gene.[5][6][7][8]

Function

The protein encoded by this gene was first identified by its binding to the APC (Adenomatous polyposis coli) protein which is often mutated in familial and sporadic forms of colorectal cancer.[9]

Immunofluorescence has demonstrated that EB1 localizes to the centrosome, mitotic spindle, and distal tips of cytoplasmic microtubules. Throughout the cell cycle, EB1 proteins situate on the microtubule plus ends, which is why EB1 is categorized as a microtubule plus end tracking protein(+TIP protein).[10]

The protein also associates with components of the dynactin complex and the intermediate chain of cytoplasmic dynein. Because of these associations, it is thought that this protein is involved in the regulation of microtubule structures and chromosome stability. This gene is a member of the RP/EB family.[8]

Interactions

MAPRE1 has been shown to interact with TERF1.[11]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101367 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027479 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Su LK, Burrell M, Hill DE, Gyuris J, Brent R, Wiltshire R, Trent J, Vogelstein B, Kinzler KW (Aug 1995). "APC binds to the novel protein EB1". Cancer Res. 55 (14): 2972–7. PMID 7606712.
  6. ^ Berrueta L, Kraeft SK, Tirnauer JS, Schuyler SC, Chen LB, Hill DE, Pellman D, Bierer BE (Sep 1998). "The adenomatous polyposis coli-binding protein EB1 is associated with cytoplasmic and spindle microtubules". Proc. Natl. Acad. Sci. USA. 95 (18): 10596–601. Bibcode:1998PNAS...9510596B. doi:10.1073/pnas.95.18.10596. PMC 27940. PMID 9724749.
  7. ^ Nakamura M, Zhou XZ, Lu KP (Jul 2001). "Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization". Curr. Biol. 11 (13): 1062–7. Bibcode:2001CBio...11.1062N. doi:10.1016/S0960-9822(01)00297-4. PMID 11470413. S2CID 14122895.
  8. ^ a b "Entrez Gene: MAPRE1 microtubule-associated protein, RP/EB family, member 1".
  9. ^ Su LK, Burrell M, Hill DE, Gyuris J, Brent R, Wiltshire R, Trent J, Vogelstein B, Kinzler KW (July 1995). "APC binds to the novel protein EB1". Cancer Research. 55 (14): 2972–7. PMID 7606712.
  10. ^ Tirnauer JS, Bierer BE (May 2000). "EB1 proteins regulate microtubule dynamics, cell polarity, and chromosome stability". The Journal of Cell Biology. 149 (4): 761–6. doi:10.1083/jcb.149.4.761. PMC 2174556. PMID 10811817.
  11. ^ Nakamura M, Zhou XZ, Kishi S, Lu KP (Mar 2002). "Involvement of the telomeric protein Pin2/TRF1 in the regulation of the mitotic spindle". FEBS Lett. 514 (2–3): 193–8. doi:10.1016/S0014-5793(02)02363-3. PMID 11943150. S2CID 2579290.

Further reading

  • Tirnauer JS, Bierer BE (2000). "EB1 proteins regulate microtubule dynamics, cell polarity, and chromosome stability". J. Cell Biol. 149 (4): 761–6. doi:10.1083/jcb.149.4.761. PMC 2174556. PMID 10811817.
  • Morrison EE, Wardleworth BN, Askham JM, Markham AF, Meredith DM (1999). "EB1, a protein which interacts with the APC tumour suppressor, is associated with the microtubule cytoskeleton throughout the cell cycle". Oncogene. 17 (26): 3471–7. doi:10.1038/sj.onc.1202247. PMID 10030671.
  • Juwana JP, Henderikx P, Mischo A, Wadle A, Fadle N, Gerlach K, Arends JW, Hoogenboom H, Pfreundschuh M, Renner C (1999). "EB/RP gene family encodes tubulin binding proteins". Int. J. Cancer. 81 (2): 275–84. doi:10.1002/(SICI)1097-0215(19990412)81:2<275::AID-IJC18>3.0.CO;2-Z. PMID 10188731. S2CID 33232892.
  • Berrueta L, Tirnauer JS, Schuyler SC, Pellman D, Bierer BE (1999). "The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain". Curr. Biol. 9 (8): 425–8. Bibcode:1999CBio....9..425B. doi:10.1016/S0960-9822(99)80190-0. PMID 10226031. S2CID 14191776.
  • Nakagawa H, Koyama K, Murata Y, Morito M, Akiyama T, Nakamura Y (2000). "EB3, a novel member of the EB1 family preferentially expressed in the central nervous system, binds to a CNS-specific APC homologue". Oncogene. 19 (2): 210–6. doi:10.1038/sj.onc.1203308. PMID 10644998.
  • Askham JM, Moncur P, Markham AF, Morrison EE (2000). "Regulation and function of the interaction between the APC tumour suppressor protein and EB1". Oncogene. 19 (15): 1950–8. doi:10.1038/sj.onc.1203498. PMID 10773885.
  • Mimori-Kiyosue Y, Shiina N, Tsukita S (2000). "The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules". Curr. Biol. 10 (14): 865–8. Bibcode:2000CBio...10..865M. doi:10.1016/S0960-9822(00)00600-X. PMID 10899006. S2CID 18926885.
  • Zhou XZ, Lu KP (2001). "The Pin2/TRF1-interacting protein PinX1 is a potent telomerase inhibitor". Cell. 107 (3): 347–59. CiteSeerX 10.1.1.326.1815. doi:10.1016/S0092-8674(01)00538-4. PMID 11701125. S2CID 6822193.
  • Nakamura M, Zhou XZ, Kishi S, Lu KP (2002). "Involvement of the telomeric protein Pin2/TRF1 in the regulation of the mitotic spindle". FEBS Lett. 514 (2–3): 193–8. doi:10.1016/S0014-5793(02)02363-3. PMID 11943150. S2CID 2579290.
  • Askham JM, Vaughan KT, Goodson HV, Morrison EE (2003). "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". Mol. Biol. Cell. 13 (10): 3627–45. doi:10.1091/mbc.E02-01-0061. PMC 129971. PMID 12388762.
  • Tirnauer JS, Canman JC, Salmon ED, Mitchison TJ (2003). "EB1 targets to kinetochores with attached, polymerizing microtubules". Mol. Biol. Cell. 13 (12): 4308–16. doi:10.1091/mbc.E02-04-0236. PMC 138635. PMID 12475954.
  • Ligon LA, Shelly SS, Tokito M, Holzbaur EL (2003). "The microtubule plus-end proteins EB1 and dynactin have differential effects on microtubule polymerization". Mol. Biol. Cell. 14 (4): 1405–17. doi:10.1091/mbc.E02-03-0155. PMC 153110. PMID 12686597.
  • Hayashi I, Ikura M (2003). "Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)". J. Biol. Chem. 278 (38): 36430–4. doi:10.1074/jbc.M305773200. PMID 12857735.
  • Bu W, Su LK (2004). "Characterization of functional domains of human EB1 family proteins". J. Biol. Chem. 278 (50): 49721–31. doi:10.1074/jbc.M306194200. PMID 14514668.
  • Bieling P, Laan L, Schek H, Munteanu EL, Sandblad L, Dogterom M, Brunner D, Surrey T (2007). "Reconstitution of a microtubule plus-end tracking system in vitro". Nature. 450 (7172): 1100–5. Bibcode:2007Natur.450.1100B. doi:10.1038/nature06386. PMID 18059460. S2CID 4355669.
  • Maurer SP, Fourniol FJ, Bohner G, Moores CA, Surrey T (2012). "EBs recognize a nucleotide-dependent structural cap at growing microtubule ends". Cell. 149 (2): 371–82. doi:10.1016/j.cell.2012.02.049. PMC 3368265. PMID 22500803.
  • Nakamura S, Grigoriev I, Nogi T, Hamaji T, Cassimeris L, Mimori-Kiyosue Y (2012). "Dissecting the nanoscale distributions and functions of microtubule-end-binding proteins EB1 and ch-TOG in interphase HeLa cells". PLOS ONE. 7 (12): e51442. Bibcode:2012PLoSO...751442N. doi:10.1371/journal.pone.0051442. PMC 3520847. PMID 23251535.
  • Zanic M, Widlund PO, Hyman AA, Howard J (2013). "Synergy between XMAP215 and EB1 increases microtubule growth rates to physiological levels". Nat. Cell Biol. 15 (6): 688–93. doi:10.1038/ncb2744. PMID 23666085. S2CID 3025200.
  • Jie, Chen (2014). "Phosphoregulation of the dimerization and functions of end-binding protein 1". Protein & Cell. 5 (10): 795–799. doi:10.1007/s13238-014-0081-9. PMC 4180461. PMID 25048701.
  • v
  • t
  • e
  • 1pa7: Crystal structure of amino-terminal microtubule binding domain of EB1
    1pa7: Crystal structure of amino-terminal microtubule binding domain of EB1
  • 1txq: Crystal structure of the EB1 C-terminal domain complexed with the CAP-Gly domain of p150Glued
    1txq: Crystal structure of the EB1 C-terminal domain complexed with the CAP-Gly domain of p150Glued
  • 1ueg: Crystal structure of amino-terminal microtubule binding domain of EB1
    1ueg: Crystal structure of amino-terminal microtubule binding domain of EB1
  • 1v5k: Solution structure of the CH domain from mouse EB-1
    1v5k: Solution structure of the CH domain from mouse EB-1
  • 1vka: Southeast Collaboratory for Structural Genomics: Hypothetical Human Protein Q15691 N-Terminal Fragment
    1vka: Southeast Collaboratory for Structural Genomics: Hypothetical Human Protein Q15691 N-Terminal Fragment
  • 1wu9: Crystal structure of the C-terminal domain of the end-binding protein 1 (EB1)
    1wu9: Crystal structure of the C-terminal domain of the end-binding protein 1 (EB1)
  • 1yib: Crystal Structure of the Human EB1 C-terminal Dimerization Domain
    1yib: Crystal Structure of the Human EB1 C-terminal Dimerization Domain
  • 1yig: Crystal Structure of the Human EB1 C-terminal Dimerization Domain
    1yig: Crystal Structure of the Human EB1 C-terminal Dimerization Domain
  • 2hkq: Crystal structure of the C-terminal domain of human EB1 in complex with the CAP-Gly domain of human Dynactin-1 (p150-Glued)
    2hkq: Crystal structure of the C-terminal domain of human EB1 in complex with the CAP-Gly domain of human Dynactin-1 (p150-Glued)
  • 2hl5: Crystal structure of the C-terminal domain of human EB1 in complex with the A49M mutant CAP-Gly domain of human Dynactin-1 (p150-Glued)
    2hl5: Crystal structure of the C-terminal domain of human EB1 in complex with the A49M mutant CAP-Gly domain of human Dynactin-1 (p150-Glued)
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Human
Microfilaments
and ABPs
Myofilament
Actins
Myosins
Other
Other
Intermediate
filaments
Type 1/2
(Keratin,
Cytokeratin)
Epithelial keratins
(soft alpha-keratins)
Hair keratins
(hard alpha-keratins)
Ungrouped alpha
Not alpha
Type 3
Type 4
Type 5
Microtubules
and MAPs
Tubulins
MAPs
Kinesins
Dyneins
Microtubule organising proteins
Microtubule severing proteins
Other
Catenins
Membrane
Other
Nonhuman
See also: cytoskeletal defects


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