Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Microtubule-associated protein RP/EB family member 3

Gene

Mapre3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plus-end tracking protein (+TIP) that 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. Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement. Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules (By similarity). May play a role in cell migration (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processCell 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi1359297. Mapre3.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002134302 – 281Microtubule-associated protein RP/EB family member 3Add BLAST280

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei162PhosphoserineCombined sources1
Modified residuei176PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ5XIT1.
PRIDEiQ5XIT1.

PTM databases

iPTMnetiQ5XIT1.
PhosphoSitePlusiQ5XIT1.

Expressioni

Gene expression databases

BgeeiENSRNOG00000008961.
GenevisibleiQ5XIT1. RN.

Interactioni

Subunit structurei

Homodimer (By similarity). Heterodimer with MAPRE1 (By similarity). Interacts with DCTN1 (By similarity). Binds to the C-terminal domain of APC (By similarity). Binds monomeric and polymerized tubulin (By similarity). Interacts (via C-terminus) with CLIP1 (By similarity). Interacts with SLAIN2 and SLAIN1 (By similarity). Interacts with APC2 (By similarity). Interacts with SRCIN1 (PubMed:19146815). Interacts with AKAP9 (By similarity). Interacts with PDE4DIP (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi256035. 1 interactor.
STRINGi10116.ENSRNOP00000011877.

Structurei

3D structure databases

ProteinModelPortaliQ5XIT1.
SMRiQ5XIT1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 116Calponin-homology (CH)Add BLAST103
Domaini194 – 264EB1 C-terminalAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni217 – 281DCTN1-bindingBy similarityAdd BLAST65
Regioni217 – 260APC-bindingBy similarityAdd BLAST44

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

Sequence similaritiesi

Belongs to the MAPRE family.Curated

Phylogenomic databases

eggNOGiKOG3000. Eukaryota.
COG5217. LUCA.
GeneTreeiENSGT00490000043329.
HOGENOMiHOG000198048.
HOVERGENiHBG052410.
InParanoidiQ5XIT1.
KOiK10436.
OMAiDSLHLTY.
OrthoDBiEOG091G0FT4.
PhylomeDBiQ5XIT1.
TreeFamiTF313620.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
InterProiView protein in InterPro
IPR036872. Calponin-like_dom_sf.
IPR001715. CH-domain.
IPR004953. EB1_C.
IPR036133. EB1_C_sf.
IPR027738. EB3.
IPR027328. MAPRE.
PANTHERiPTHR10623. PTHR10623. 1 hit.
PTHR10623:SF10. PTHR10623:SF10. 1 hit.
PfamiView protein in Pfam
PF00307. CH. 1 hit.
PF03271. EB1. 1 hit.
SUPFAMiSSF140612. SSF140612. 1 hit.
SSF47576. SSF47576. 1 hit.
PROSITEiView protein in PROSITE
PS50021. CH. 1 hit.
PS51230. EB1_C. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5XIT1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVNVYSTSV TSENLSRHDM LAWVNDSLHL NYTKIEQLCS GAAYCQFMDM
60 70 80 90 100
LFPGCVHLRK VKFQAKLEHE YIHNFKVLQA AFKKMGVDKI IPVEKLVKGK
110 120 130 140 150
FQDNFEFIQW FKKFFDANYD GKDYNPLLAR QGQDVAPPPN PGDQIFNKSK
160 170 180 190 200
KLIGTAVPQR TSPTGPKNMQ TSGRLSNVAP PCILRKNPPS ARNGGHEADA
210 220 230 240 250
QILELNQQLL DLKLTVDGLE KERDFYFSKL RDIELICQEH ESENSPVISG
260 270 280
IIGILYATEE GFAPPEDDEI EEHQQEDQDE Y
Length:281
Mass (Da):31,966
Last modified:November 23, 2004 - v1
Checksum:i6713427C480838DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083589 mRNA. Translation: AAH83589.1.
RefSeqiNP_001007657.1. NM_001007656.1.
XP_008762734.1. XM_008764512.2.
UniGeneiRn.154513.

Genome annotation databases

EnsembliENSRNOT00000011874; ENSRNOP00000011877; ENSRNOG00000008961.
GeneIDi298848.
KEGGirno:298848.

Similar proteinsi

Entry informationi

Entry nameiMARE3_RAT
AccessioniPrimary (citable) accession number: Q5XIT1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 23, 2004
Last modified: November 22, 2017
This is version 109 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families