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Protein

Microtubule-associated protein RP/EB family member 1

Gene

MAPRE1

Organism
Homo sapiens (Human)
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. May play a role in cell migration.4 Publications

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • microtubule plus-end binding Source: UniProtKB
  • protein C-terminus binding Source: ProtInc
  • RNA binding Source: UniProtKB

GO - Biological processi

Keywordsi

Biological processCell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-141444. Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-380284. Loss of proteins required for interphase microtubule organization from the centrosome.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854518. AURKA Activation by TPX2.
SIGNORiQ15691.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

EuPathDBiHostDB:ENSG00000101367.8.
HGNCiHGNC:6890. MAPRE1.

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi59 – 60KK → EE: No effect. 1 Publication2
Mutagenesisi89K → E: Loss of binding to microtubules. 1 Publication1

Organism-specific databases

DisGeNETi22919.
OpenTargetsiENSG00000101367.
PharmGKBiPA30634.

Polymorphism and mutation databases

BioMutaiMAPRE1.
DMDMi20138589.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00002134162 – 268Microtubule-associated protein RP/EB family member 1Add BLAST267

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei124PhosphotyrosineCombined sources1
Modified residuei155PhosphoserineCombined sources1
Modified residuei165PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ15691.
MaxQBiQ15691.
PaxDbiQ15691.
PeptideAtlasiQ15691.
PRIDEiQ15691.

2D gel databases

OGPiQ15691.
REPRODUCTION-2DPAGEiIPI00017596.

PTM databases

iPTMnetiQ15691.
PhosphoSitePlusiQ15691.
SwissPalmiQ15691.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000101367.
CleanExiHS_MAPRE1.
GenevisibleiQ15691. HS.

Organism-specific databases

HPAiCAB009337.
CAB019391.
HPA003600.

Interactioni

Subunit structurei

Homodimer (PubMed:15616574). Heterodimer with MAPRE3 (PubMed:19255245). Interacts with DCTN1, DCTN2, TERF1 and dynein intermediate chain (PubMed:10226031, PubMed:11943150, PubMed:12388762, PubMed:14514668, PubMed:16109370, PubMed:16949363, PubMed:23874158). Interaction with DIAPH1 and DIAPH2 (By similarity). Interacts with APC (via C-terminal domain), CLASP2, DST, KIF2C and STIM1; probably required for their targeting to the growing microtubule plus ends (PubMed:12388762, PubMed:14514668, PubMed:15616574, PubMed:15631994, PubMed:19543227, PubMed:19632184, PubMed:7606712). Interacts with MTUS2; interaction is direct and probably targets MTUS2 to microtubules (PubMed:19543227). Interacts with APC2 (PubMed:10644998). Interacts with CLASP1 (PubMed:15631994). Interacts with CDK5RAP2 (PubMed:19553473). Interacts with MACF1 (By similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (By similarity). Interacts with KCNAB2 (By similarity). Interacts (via C-terminus) with CLIP1 (PubMed:21646404, PubMed:17563362). Interacts with SLAIN2 and SLAIN1 (PubMed:21646404). Interacts with KIF18B; this interaction is required for efficient accumulation of KIF18B at microtubule plus ends (PubMed:21820309). Interacts with MISP (PubMed:23509069). Interacts with KNSTRN (PubMed:23035123). Interacts with NCKAP5L (PubMed:26485573).By similarity22 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • microtubule plus-end binding Source: UniProtKB
  • protein C-terminus binding Source: ProtInc

Protein-protein interaction databases

BioGridi116581. 170 interactors.
DIPiDIP-38018N.
ELMiQ15691.
IntActiQ15691. 136 interactors.
MINTiMINT-206298.
STRINGi9606.ENSP00000364721.

Structurei

Secondary structure

1268
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 28Combined sources12
Helixi35 – 40Combined sources6
Helixi42 – 51Combined sources10
Helixi58 – 60Combined sources3
Helixi68 – 85Combined sources18
Helixi93 – 96Combined sources4
Turni97 – 99Combined sources3
Helixi101 – 118Combined sources18
Helixi126 – 129Combined sources4
Helixi192 – 230Combined sources39
Turni231 – 233Combined sources3
Helixi237 – 247Combined sources11
Helixi251 – 253Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PA7X-ray1.45A1-130[»]
1TXQX-ray1.80B183-268[»]
1UEGX-ray2.40A1-130[»]
1VKAX-ray1.60A/B2-140[»]
1WU9X-ray1.54A/B191-268[»]
1YIBX-ray1.80A185-255[»]
1YIGX-ray2.00A/B185-255[»]
2HKQX-ray1.86A191-268[»]
2HL3X-ray2.03C263-268[»]
2HL5X-ray1.93A/B191-268[»]
2QJZX-ray1.25A/B12-133[»]
2R8UX-ray1.35A/B1-268[»]
3GJOX-ray2.50A/B/C/D191-260[»]
3MTUX-ray2.10A/B/C/D215-257[»]
3MUDX-ray2.20C/D226-257[»]
3TQ7X-ray2.30A191-268[»]
4XA1X-ray3.20A/B/C/D211-251[»]
4XA3X-ray2.55A/B215-251[»]
4XA6X-ray3.42A/B/C/D209-251[»]
5JV3X-ray2.01A/B/C/D210-257[»]
5JVMX-ray1.57A/B207-257[»]
5JVPX-ray2.10A/B/C/D/E/F210-257[»]
5JVRX-ray2.10A/B/C/D/E/F/G/H207-257[»]
5JVSX-ray2.25A207-257[»]
5JVUX-ray1.95A/B207-257[»]
5JX1X-ray1.67A210-257[»]
5WLQX-ray3.10A208-257[»]
ProteinModelPortaliQ15691.
SMRiQ15691.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15691.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 116Calponin-homology (CH)PROSITE-ProRule annotationAdd BLAST103
Domaini185 – 255EB1 C-terminalPROSITE-ProRule annotationAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni124 – 268Interaction with MTUS2/TIP1501 PublicationAdd BLAST145
Regioni185 – 268Interaction with CDK5RAP21 PublicationAdd BLAST84
Regioni208 – 268DCTN1-bindingAdd BLAST61
Regioni220 – 242APC-bindingAdd BLAST23

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

Phylogenomic databases

eggNOGiKOG3000. Eukaryota.
COG5217. LUCA.
GeneTreeiENSGT00490000043329.
HOGENOMiHOG000198048.
HOVERGENiHBG052410.
InParanoidiQ15691.
KOiK10436.
OMAiCQVFDSI.
OrthoDBiEOG091G0FT4.
PhylomeDBiQ15691.
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.
IPR027739. EB1_Meta.
IPR027328. MAPRE.
PANTHERiPTHR10623. PTHR10623. 1 hit.
PTHR10623:SF20. PTHR10623:SF20. 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.

Q15691-1 [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 GKDYDPVAAR QGQETAVAPS LVAPALNKPK
160 170 180 190 200
KPLTSSSAAP QRPISTQRTA AAPKAGPGVV RKNPGVGNGD DEAAELMQQV
210 220 230 240 250
NVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ RIVDILYATD
260
EGFVIPDEGG PQEEQEEY
Length:268
Mass (Da):29,999
Last modified:January 23, 2007 - v3
Checksum:i08C8999F45A145ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24166 mRNA. Translation: AAC09471.1.
AK312590 mRNA. Translation: BAG35484.1.
AL035071 Genomic DNA. Translation: CAB53072.1.
CH471077 Genomic DNA. Translation: EAW76348.1.
CH471077 Genomic DNA. Translation: EAW76349.1.
BC106068 mRNA. Translation: AAI06069.1.
BC109281 mRNA. Translation: AAI09282.1.
CCDSiCCDS13208.1.
PIRiI52726.
RefSeqiNP_036457.1. NM_012325.2.
XP_011526998.1. XM_011528696.2.
UniGeneiHs.472437.

Genome annotation databases

EnsembliENST00000375571; ENSP00000364721; ENSG00000101367.
GeneIDi22919.
KEGGihsa:22919.
UCSCiuc002wyh.3. human.

Similar proteinsi

Entry informationi

Entry nameiMARE1_HUMAN
AccessioniPrimary (citable) accession number: Q15691
Secondary accession number(s): B2R6I7, E1P5M8, Q3KQS8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 188 of the entry and version 3 of the sequence. See 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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