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Protein

Microtubule-associated protein RP/EB family member 1

Gene

Mapre1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (By similarity). May play a role in cell migration.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:891995. Mapre1.

Subcellular locationi

GO - Cellular componenti

  • cell projection Source: MGI
  • cell projection membrane Source: MGI
  • centrosome Source: MGI
  • cortical microtubule cytoskeleton Source: UniProtKB
  • cytoplasm Source: MGI
  • Golgi apparatus Source: MGI
  • microtubule Source: UniProtKB
  • microtubule cytoskeleton Source: MGI
  • spindle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi211 – 2155EKERD → KKERK: Loss of interaction with APC and DCTN1. 1 Publication
Mutagenesisi211 – 2133EKE → AKA: Partial loss of interaction with APC. 1 Publication
Mutagenesisi220 – 2223KLR → ALA: Loss of interaction with APC and DCTN1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 268267Microtubule-associated protein RP/EB family member 1PRO_0000213417Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei124 – 1241PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ61166.
MaxQBiQ61166.
PaxDbiQ61166.
PRIDEiQ61166.

2D gel databases

REPRODUCTION-2DPAGEQ61166.

PTM databases

iPTMnetiQ61166.
PhosphoSiteiQ61166.
SwissPalmiQ61166.

Expressioni

Tissue specificityi

Expressed within the midpiece of sperm tail (at protein level).1 Publication

Gene expression databases

BgeeiQ61166.
ExpressionAtlasiQ61166. baseline and differential.
GenevisibleiQ61166. MM.

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 (via C-terminus) with CLIP1. Interacts with SLAIN2 (PubMed:21646404). According to PubMed:19553473, MAPRE1 does not interact with CDK5RAP2. Interacts with MACF1 (PubMed:18854161). Interacts with KIF18B; this interaction is required for efficient accumulation of KIF18B at microtubule plus ends (By similarity). Interacts with MISP (By similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (PubMed:23055941). Interacts with KCNAB2 (PubMed:21357749). Interacts with KNSTRN. Interacts with NCKAP5L (By similarity).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DSTQ030014EBI-2027055,EBI-310758From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199356. 24 interactions.
DIPiDIP-46795N.
IntActiQ61166. 28 interactions.
MINTiMINT-4101226.
STRINGi10090.ENSMUSP00000028981.

Structurei

Secondary structure

1
268
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 173Combined sources
Helixi18 – 2811Combined sources
Beta strandi33 – 353Combined sources
Helixi36 – 383Combined sources
Beta strandi39 – 413Combined sources
Helixi43 – 519Combined sources
Turni58 – 603Combined sources
Helixi68 – 8518Combined sources
Turni94 – 974Combined sources
Helixi105 – 11612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V5KNMR-A15-116[»]
ProteinModelPortaliQ61166.
SMRiQ61166. Positions 1-132, 191-257.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61166.

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/TIP150By similarityAdd
BLAST
Regioni208 – 26861DCTN1-bindingBy similarityAdd
BLAST
Regioni220 – 24223APC-bindingBy similarityAdd
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 (By similarity).By similarity

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

eggNOGiKOG3000. Eukaryota.
COG5217. LUCA.
GeneTreeiENSGT00490000043329.
HOGENOMiHOG000198048.
HOVERGENiHBG052410.
InParanoidiQ61166.
KOiK10436.
OMAiPMSTQRT.
OrthoDBiEOG7ZD1W5.
PhylomeDBiQ61166.
TreeFamiTF313620.

Family and domain databases

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

Q61166-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GAAYCQFMDM
60 70 80 90 100
LFPGSIALKK VKFQAKLEHE YIQNFKILQA GFKRMGVDKI IPVDKLVKGK
110 120 130 140 150
FQDNFEFVQW FKKFFDANYD GKEYDPVAAR QGQETAVAPS LVAPALSKPK
160 170 180 190 200
KPLGSSTAAP QRPIATQRTT AAPKAGPGMV RKNPGVGNGD DEAAELMQQV
210 220 230 240 250
KVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ RIVDILYATD
260
EGFVIPDEGG PQEEQEEY
Length:268
Mass (Da):30,016
Last modified:January 23, 2007 - v3
Checksum:i8FE3AFB7A5AE7762
GO

Sequence cautioni

The sequence AAH52405.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51196 mRNA. Translation: AAA96320.1.
BC052405 mRNA. Translation: AAH52405.1. Different initiation.
BC064444 mRNA. Translation: AAH64444.1.
CCDSiCCDS16917.1.
RefSeqiNP_031922.1. NM_007896.3.
UniGeneiMm.143877.

Genome annotation databases

EnsembliENSMUST00000028981; ENSMUSP00000028981; ENSMUSG00000027479.
GeneIDi13589.
KEGGimmu:13589.
UCSCiuc008nik.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51196 mRNA. Translation: AAA96320.1.
BC052405 mRNA. Translation: AAH52405.1. Different initiation.
BC064444 mRNA. Translation: AAH64444.1.
CCDSiCCDS16917.1.
RefSeqiNP_031922.1. NM_007896.3.
UniGeneiMm.143877.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V5KNMR-A15-116[»]
ProteinModelPortaliQ61166.
SMRiQ61166. Positions 1-132, 191-257.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199356. 24 interactions.
DIPiDIP-46795N.
IntActiQ61166. 28 interactions.
MINTiMINT-4101226.
STRINGi10090.ENSMUSP00000028981.

PTM databases

iPTMnetiQ61166.
PhosphoSiteiQ61166.
SwissPalmiQ61166.

2D gel databases

REPRODUCTION-2DPAGEQ61166.

Proteomic databases

EPDiQ61166.
MaxQBiQ61166.
PaxDbiQ61166.
PRIDEiQ61166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028981; ENSMUSP00000028981; ENSMUSG00000027479.
GeneIDi13589.
KEGGimmu:13589.
UCSCiuc008nik.1. mouse.

Organism-specific databases

CTDi22919.
MGIiMGI:891995. Mapre1.

Phylogenomic databases

eggNOGiKOG3000. Eukaryota.
COG5217. LUCA.
GeneTreeiENSGT00490000043329.
HOGENOMiHOG000198048.
HOVERGENiHBG052410.
InParanoidiQ61166.
KOiK10436.
OMAiPMSTQRT.
OrthoDBiEOG7ZD1W5.
PhylomeDBiQ61166.
TreeFamiTF313620.

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Miscellaneous databases

EvolutionaryTraceiQ61166.
NextBioi284194.
PROiQ61166.
SOURCEiSearch...

Gene expression databases

BgeeiQ61166.
ExpressionAtlasiQ61166. baseline and differential.
GenevisibleiQ61166. MM.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR004953. EB1_C.
IPR027328. MAPRE.
[Graphical view]
PANTHERiPTHR10623. PTHR10623. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Sparks A.B., Kay B.K.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17; 77-84; 114-150 AND 205-214, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic fibroblast.
  4. "EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration."
    Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J.S., Chen M., Wallar B.J., Alberts A.S., Gundersen G.G.
    Nat. Cell Biol. 6:820-830(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APC; DCTN1; DIAPH1 AND DIAPH2, MUTAGENESIS OF 211-GLU--GLU-213; 211-GLU--ASP-215 AND 220-LYS--ARG-222, FUNCTION.
  5. "ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity."
    Wu X., Kodama A., Fuchs E.
    Cell 135:137-148(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MACF1.
  6. "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: SUBUNIT.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "Cdk-mediated phosphorylation of the Kvbeta2 auxiliary subunit regulates Kv1 channel axonal targeting."
    Vacher H., Yang J.W., Cerda O., Autillo-Touati A., Dargent B., Trimmer J.S.
    J. Cell Biol. 192:813-824(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNAB2, SUBCELLULAR LOCATION.
  9. "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.
  10. "RAB-like 2 has an essential role in male fertility, sperm intra-flagellar transport, and tail assembly."
    Lo J.C., Jamsai D., O'Connor A.E., Borg C., Clark B.J., Whisstock J.C., Field M.C., Adams V., Ishikawa T., Aitken R.J., Whittle B., Goodnow C.C., Ormandy C.J., O'Bryan M.K.
    PLoS Genet. 8:E1002969-E1002969(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RABL2, TISSUE SPECIFICITY.
  11. "Solution structure of the CH domain from mouse EB-1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAY-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 12-117.

Entry informationi

Entry nameiMARE1_MOUSE
AccessioniPrimary (citable) accession number: Q61166
Secondary accession number(s): Q7TN34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.