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Protein

Microtubule-associated protein RP/EB family member 2

Gene

Mapre2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein RP/EB family member 2
Gene namesi
Name:Mapre2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1590736. Mapre2.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmcytoskeleton By similarity

  • Note: Associated with the microtubule network. Accumulates at the plus end of microtubules (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Microtubule-associated protein RP/EB family member 2PRO_0000240312Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineCombined sources
Modified residuei166 – 1661PhosphotyrosineBy similarity
Modified residuei218 – 2181PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ3B8Q0.
PRIDEiQ3B8Q0.

PTM databases

iPTMnetiQ3B8Q0.
PhosphoSiteiQ3B8Q0.

Interactioni

Subunit structurei

Interacts with DCTN1. Binds to the C-terminal domain of APC. Binds monomeric and polymerized tubulin (By similarity).By similarity

Protein-protein interaction databases

BioGridi594167. 1 interaction.
IntActiQ3B8Q0. 1 interaction.
STRINGi10116.ENSRNOP00000065460.

Structurei

3D structure databases

ProteinModelPortaliQ3B8Q0.
SMRiQ3B8Q0. Positions 38-191, 245-301.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 158103CHPROSITE-ProRule annotationAdd
BLAST
Domaini235 – 30571EB1 C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 326141DCTN1-bindingBy similarityAdd
BLAST
Regioni258 – 30144APC-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.
HOVERGENiHBG052410.
InParanoidiQ3B8Q0.
KOiK10436.
PhylomeDBiQ3B8Q0.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR004953. EB1_C.
IPR027328. MAPRE.
IPR027735. RP1/EB2_vertebrate.
[Graphical view]
PANTHERiPTHR10623. PTHR10623. 1 hit.
PTHR10623:SF7. PTHR10623:SF7. 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.

Q3B8Q0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGPTQTLSP NGENNNDIIQ DNGTIIPFRK HTVRGERSYS WGMAVNVYST
60 70 80 90 100
SITQETMSRH DIIAWVNDIV SLNYTKVEQL CSGAAYCQFM DMLFPGCISL
110 120 130 140 150
KKVKFQAKLE HEYIHNFKLL QASFKRMNVD KVIPVEKLVK GRFQDNLDFI
160 170 180 190 200
QWFKKFYDAN YDGKEYDPVE ARQGQDAIPP PDPGEQIFNL PKKSHHANSP
210 220 230 240 250
TAGAAKSSPA AKPGSTPSRP SSAKRASSSG SASRSDKDLE TQVIQLNEQV
260 270 280 290 300
HSLKLALEGV EKERDFYFGK LREIELLCQE HGQENDDLVQ RLMEVLYASD
310 320
EQEGQTEEPE VEEQTHDQQP QQQEEY
Length:326
Mass (Da):36,988
Last modified:November 22, 2005 - v1
Checksum:i86829172C9E75643
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC105879 mRNA. Translation: AAI05880.1.
RefSeqiNP_001094470.1. NM_001101000.1.
UniGeneiRn.154513.

Genome annotation databases

GeneIDi679221.
KEGGirno:679221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC105879 mRNA. Translation: AAI05880.1.
RefSeqiNP_001094470.1. NM_001101000.1.
UniGeneiRn.154513.

3D structure databases

ProteinModelPortaliQ3B8Q0.
SMRiQ3B8Q0. Positions 38-191, 245-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi594167. 1 interaction.
IntActiQ3B8Q0. 1 interaction.
STRINGi10116.ENSRNOP00000065460.

PTM databases

iPTMnetiQ3B8Q0.
PhosphoSiteiQ3B8Q0.

Proteomic databases

PaxDbiQ3B8Q0.
PRIDEiQ3B8Q0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi679221.
KEGGirno:679221.

Organism-specific databases

CTDi10982.
RGDi1590736. Mapre2.

Phylogenomic databases

eggNOGiKOG3000. Eukaryota.
COG5217. LUCA.
HOVERGENiHBG052410.
InParanoidiQ3B8Q0.
KOiK10436.
PhylomeDBiQ3B8Q0.

Miscellaneous databases

NextBioi716023.
PROiQ3B8Q0.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR004953. EB1_C.
IPR027328. MAPRE.
IPR027735. RP1/EB2_vertebrate.
[Graphical view]
PANTHERiPTHR10623. PTHR10623. 1 hit.
PTHR10623:SF7. PTHR10623:SF7. 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

  1. "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].
    Tissue: Lung.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMARE2_RAT
AccessioniPrimary (citable) accession number: Q3B8Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: November 22, 2005
Last modified: January 20, 2016
This is version 74 of the entry and version 1 of the sequence. [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

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.