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Q15691

- MARE1_HUMAN

UniProt

Q15691 - MARE1_HUMAN

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Protein

Microtubule-associated protein RP/EB family member 1

Gene

MAPRE1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. microtubule plus-end binding Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB
  3. protein C-terminus binding Source: ProtInc

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. G2/M transition of mitotic cell cycle Source: Reactome
  3. mitotic cell cycle Source: Reactome
  4. mitotic nuclear division Source: UniProtKB-KW
  5. negative regulation of microtubule polymerization Source: UniProtKB
  6. positive regulation of microtubule plus-end binding Source: Ensembl
  7. protein localization to microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_682. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:6890. MAPRE1.

Subcellular locationi

Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
Note: Associated with the microtubule network at the growing distal tip of microtubules. Also enriched at the centrosome.

GO - Cellular componenti

  1. cell projection membrane Source: Ensembl
  2. centrosome Source: UniProtKB
  3. cortical microtubule cytoskeleton Source: UniProtKB
  4. cytoplasm Source: HPA
  5. cytoplasmic microtubule Source: Ensembl
  6. cytosol Source: Reactome
  7. Golgi apparatus Source: Ensembl
  8. microtubule Source: UniProtKB
  9. microtubule plus-end Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 602KK → EE: No effect. 1 Publication
Mutagenesisi89 – 891K → E: Loss of binding to microtubules. 1 Publication

Organism-specific databases

PharmGKBiPA30634.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 268267Microtubule-associated protein RP/EB family member 1PRO_0000213416Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei124 – 1241Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15691.
PaxDbiQ15691.
PeptideAtlasiQ15691.
PRIDEiQ15691.

2D gel databases

OGPiQ15691.
REPRODUCTION-2DPAGEIPI00017596.

PTM databases

PhosphoSiteiQ15691.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ15691.
CleanExiHS_MAPRE1.
GenevestigatoriQ15691.

Organism-specific databases

HPAiCAB009337.
CAB019391.
HPA003600.

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 with CDK5RAP2. Interacts with MACF1 (By similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (By similarity). Interacts (via C-terminus) with CLIP1. Interacts with SLAIN2. Interacts with KIF18B; this interaction is required for efficient accumulation of KIF18B at microtubule plus ends. Interacts with MISP.By similarity19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APCP250544EBI-1004115,EBI-727707
APC2O959963EBI-1004115,EBI-1053045
DSTQ030012EBI-1004115,EBI-310758
KIF2CQ996615EBI-1004115,EBI-1642317
MTUS2Q5JR597EBI-1004115,EBI-742948
TERF1P542742EBI-1004115,EBI-710997

Protein-protein interaction databases

BioGridi116581. 49 interactions.
DIPiDIP-38018N.
IntActiQ15691. 19 interactions.
MINTiMINT-206298.
STRINGi9606.ENSP00000364721.

Structurei

Secondary structure

1
268
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 2812
Helixi35 – 406
Helixi42 – 5110
Helixi58 – 603
Helixi68 – 8518
Helixi93 – 964
Turni97 – 993
Helixi101 – 11818
Helixi126 – 1294
Helixi192 – 23039
Turni231 – 2333
Helixi237 – 24711
Beta strandi250 – 2523

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
3TQ7X-ray2.30A191-268[»]
ProteinModelPortaliQ15691.
SMRiQ15691. Positions 1-132, 191-257.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15691.

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/TIP150Add
BLAST
Regioni185 – 26884Interaction with CDK5RAP2Add
BLAST
Regioni208 – 26861DCTN1-bindingAdd
BLAST
Regioni220 – 24223APC-bindingAdd
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.

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

eggNOGiCOG5217.
GeneTreeiENSGT00490000043329.
HOGENOMiHOG000198048.
HOVERGENiHBG052410.
InParanoidiQ15691.
KOiK10436.
OMAiATPPNRM.
OrthoDBiEOG7ZD1W5.
PhylomeDBiQ15691.
TreeFamiTF313620.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR004953. EB1_C.
IPR027739. EB1_vertebrate.
IPR027328. MAPRE.
[Graphical view]
PANTHERiPTHR10623. PTHR10623. 1 hit.
PTHR10623:SF13. PTHR10623:SF13. 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.

Q15691 [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:
EMBL
GenBank
DDBJ
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.
UniGeneiHs.472437.

Genome annotation databases

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

Polymorphism databases

DMDMi20138589.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS13208.1.
PIRi I52726.
RefSeqi NP_036457.1. NM_012325.2.
UniGenei Hs.472437.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PA7 X-ray 1.45 A 1-130 [» ]
1TXQ X-ray 1.80 B 183-268 [» ]
1UEG X-ray 2.40 A 1-130 [» ]
1VKA X-ray 1.60 A/B 2-140 [» ]
1WU9 X-ray 1.54 A/B 191-268 [» ]
1YIB X-ray 1.80 A 185-255 [» ]
1YIG X-ray 2.00 A/B 185-255 [» ]
2HKQ X-ray 1.86 A 191-268 [» ]
2HL3 X-ray 2.03 C 263-268 [» ]
2HL5 X-ray 1.93 A/B 191-268 [» ]
2QJZ X-ray 1.25 A/B 12-133 [» ]
2R8U X-ray 1.35 A/B 1-268 [» ]
3GJO X-ray 2.50 A/B/C/D 191-260 [» ]
3MTU X-ray 2.10 A/B/C/D 215-257 [» ]
3TQ7 X-ray 2.30 A 191-268 [» ]
ProteinModelPortali Q15691.
SMRi Q15691. Positions 1-132, 191-257.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116581. 49 interactions.
DIPi DIP-38018N.
IntActi Q15691. 19 interactions.
MINTi MINT-206298.
STRINGi 9606.ENSP00000364721.

PTM databases

PhosphoSitei Q15691.

Polymorphism databases

DMDMi 20138589.

2D gel databases

OGPi Q15691.
REPRODUCTION-2DPAGE IPI00017596.

Proteomic databases

MaxQBi Q15691.
PaxDbi Q15691.
PeptideAtlasi Q15691.
PRIDEi Q15691.

Protocols and materials databases

DNASUi 22919.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375571 ; ENSP00000364721 ; ENSG00000101367 .
GeneIDi 22919.
KEGGi hsa:22919.
UCSCi uc002wyh.3. human.

Organism-specific databases

CTDi 22919.
GeneCardsi GC20P031407.
HGNCi HGNC:6890. MAPRE1.
HPAi CAB009337.
CAB019391.
HPA003600.
MIMi 603108. gene.
neXtProti NX_Q15691.
PharmGKBi PA30634.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5217.
GeneTreei ENSGT00490000043329.
HOGENOMi HOG000198048.
HOVERGENi HBG052410.
InParanoidi Q15691.
KOi K10436.
OMAi ATPPNRM.
OrthoDBi EOG7ZD1W5.
PhylomeDBi Q15691.
TreeFami TF313620.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSi MAPRE1. human.
EvolutionaryTracei Q15691.
GeneWikii MAPRE1.
GenomeRNAii 22919.
NextBioi 43617.
PROi Q15691.
SOURCEi Search...

Gene expression databases

Bgeei Q15691.
CleanExi HS_MAPRE1.
Genevestigatori Q15691.

Family and domain databases

Gene3Di 1.10.418.10. 1 hit.
InterProi IPR001715. CH-domain.
IPR004953. EB1_C.
IPR027739. EB1_vertebrate.
IPR027328. MAPRE.
[Graphical view ]
PANTHERi PTHR10623. PTHR10623. 1 hit.
PTHR10623:SF13. PTHR10623:SF13. 1 hit.
Pfami PF00307. CH. 1 hit.
PF03271. EB1. 1 hit.
[Graphical view ]
SUPFAMi SSF140612. SSF140612. 1 hit.
SSF47576. SSF47576. 1 hit.
PROSITEi PS50021. CH. 1 hit.
PS51230. EB1_C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "APC binds to the novel protein EB1."
    Su L.-K., Burrell M., Hill D.E., Gyuris J., Brent R., Wiltshire R., Trent J., Vogelstein B., Kinzler K.W.
    Cancer Res. 55:2972-2977(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH APC.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
  6. Bienvenut W.V., Potts A., Barblan J., Quadroni M.
    Submitted (JUL-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  7. "The adenomatous polyposis coli-binding protein EB1 is associated with cytoplasmic and spindle microtubules."
    Berrueta L., Kraeft S.-K., Tirnauer J.S., Schuyler S.C., Chen L.B., Hill D.E., Pellman D., Bierer B.E.
    Proc. Natl. Acad. Sci. U.S.A. 95:10596-10601(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain."
    Berrueta L., Tirnauer J.S., Schuyler S.C., Pellman D., Bierer B.E.
    Curr. Biol. 9:425-428(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCTN1; DCTN2 AND DYNEIN INTERMEDIATE CHAIN.
  9. Cited for: INTERACTION WITH TUBULIN.
  10. "EB3, a novel member of the EB1 family preferentially expressed in the central nervous system, binds to a CNS-specific APC homologue."
    Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.
    Oncogene 19:210-216(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APC2, TISSUE SPECIFICITY.
  11. "Involvement of the telomeric protein Pin2/TRF1 in the regulation of the mitotic spindle."
    Nakamura M., Zhen Zhou X., Kishi S., Ping Lu K.
    FEBS Lett. 514:193-198(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TERF1.
  12. "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."
    Askham J.M., Vaughan K.T., Goodson H.V., Morrison E.E.
    Mol. Biol. Cell 13:3627-3645(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APC AND DCTN1, SUBCELLULAR LOCATION, FUNCTION.
  13. "Characterization of functional domains of human EB1 family proteins."
    Bu W., Su L.-K.
    J. Biol. Chem. 278:49721-49731(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, INTERACTION WITH TUBULIN; APC AND DCTN1.
  14. "CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics at the cell cortex."
    Mimori-Kiyosue Y., Grigoriev I., Lansbergen G., Sasaki H., Matsui C., Severin F., Galjart N., Grosveld F., Vorobjev I., Tsukita S., Akhmanova A.
    J. Cell Biol. 168:141-153(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLASP1 AND CLASP2.
  15. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition."
    Mishima M., Maesaki R., Kasa M., Watanabe T., Fukata M., Kaibuchi K., Hakoshima T.
    Proc. Natl. Acad. Sci. U.S.A. 104:10346-10351(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLIP1.
  17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "TIP150 interacts with and targets MCAK at the microtubule plus ends."
    Jiang K., Wang J., Liu J., Ward T., Wordeman L., Davidson A., Wang F., Yao X.
    EMBO Rep. 10:857-865(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MTUS2 AND KIF2C.
  19. Cited for: INTERACTION WITH MAPRE3.
  20. "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: INTERACTION WITH CDK5RAP2.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "A complex of Kif18b and MCAK promotes microtubule depolymerization and is negatively regulated by Aurora kinases."
    Tanenbaum M.E., Macurek L., van der Vaart B., Galli M., Akhmanova A., Medema R.H.
    Curr. Biol. 21:1356-1365(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIF18B.
  23. "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 AND CLIP1, FUNCTION, SUBCELLULAR LOCATION.
  24. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "MISP is a novel Plk1 substrate required for proper spindle orientation and mitotic progression."
    Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P., Goenczy P., Hoffmann I.
    J. Cell Biol. 200:773-787(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MISP.
  27. Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 191-268, DIMERIZATION, INTERACTION WITH APC.
  28. "Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)."
    Hayashi I., Ikura M.
    J. Biol. Chem. 278:36430-36434(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-130, MUTAGENESIS OF 59-LYS-LYS-60 AND LYS-89.
  29. "Structural basis for the activation of microtubule assembly by the EB1 and p150Glued complex."
    Hayashi I., Wilde A., Mal T.K., Ikura M.
    Mol. Cell 19:449-460(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 183-268 IN COMPLEX WITH DCTN1, FUNCTION, SUBUNIT, INTERACTION WITH DCTN1, SUBCELLULAR LOCATION.
  30. Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 191-267 IN COMPLEX WITH DCTN1.
  31. "Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1."
    Slep K.C., Vale R.D.
    Mol. Cell 27:976-991(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 12-133.
  32. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 191-260 IN COMPLEX WITH DST, FUNCTION, INTERACTION WITH APC; CLASP2; KIF2C AND STIM1, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiMARE1_HUMAN
AccessioniPrimary (citable) accession number: Q15691
Secondary accession number(s): B2R6I7, E1P5M8, Q3KQS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 155 of the entry and version 3 of the sequence. [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

External Data

Dasty 3