Reviewed, UniProtKB/Swiss-Prot Q15691 (MARE1_HUMAN)

Names and origin

Protein names

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 names

Name:

MAPRE1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	268 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration. Ref.10
Subunit structure	Homodimer. Interacts with DCTN1, DCTN2, DIAPH1, DIAPH2, TERF1 and dynein intermediate chain. Binds to the C-terminal domain of APC and interacts with APC2. Interacts with CLASP1 and CLASP2. Ref.10 Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.16
Subcellular location	Cytoplasm. Note: Associated with the microtubule network at the growing distal tip of microtubules. Also enriched at the centrosome. Ref.10 Ref.5
Tissue specificity	Ubiquitously expressed. Ref.8
Domain	Composed of two functionally independent domains. The N-terminal domain forms an hydrophobic cleft involved in microtubule binding and the C-terminal is involved in the formation of mutually exclusive complexes with APC and DCTN1.
Sequence similarities	Belongs to the MAPRE family. Contains 1 CH (calponin-homology) domain. Contains 1 EB1 C-terminal domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Microtubule
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Ref.1 Traceable author statement. Source: ProtInc mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of microtubule polymerization Ref.9 Inferred from direct assay. Source: UniProtKB
Cellular component	cortical microtubule cytoskeleton Ref.12 Inferred from direct assay. Source: UniProtKB
Molecular function	microtubule plus-end binding Ref.12 Inferred from direct assay. Source: UniProtKB protein C-terminus binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APC	P25054	1	EBI-1004115,EBI-727707
TERF1	P54274	2	EBI-1004115,EBI-710997
TERF1	P54274-2	1	EBI-1004115,EBI-711018

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 268

267

Microtubule-associated protein RP/EB family member 1

PRO_0000213416

Regions

Domain

14 – 116

103

CH

Domain

185 – 255

71

EB1 C-terminal

Region

208 – 268

61

DCTN1-binding

Region

220 – 242

23

APC-binding

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.4

Modified residue

124

1

Phosphotyrosine Ref.13

Modified residue

155

1

Phosphoserine Ref.14

Modified residue

166

1

Phosphothreonine Ref.14

Experimental info

Mutagenesis

59 – 60

2

KK → EE: No effect.

Mutagenesis

89

1

K → E: Loss of binding to microtubules. Ref.17

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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268

Helix Strand Turn

Details...

Helix

17 – 28

12

Helix

35 – 40

6

Helix

42 – 51

10

Helix

58 – 60

3

Helix

68 – 85

18

Helix

93 – 96

4

Helix

101 – 118

18

Turn

126 – 129

4

Helix

193 – 230

38

Turn

231 – 233

3

Helix

237 – 246

10

Beta strand

250 – 252

3

Sequences

	Sequence		Length	Mass (Da)
	Q15691-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 08C8999F45A145ED	FASTA	268	29,999
	10 20 30 40 50 60 MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GAAYCQFMDM LFPGSIALKK 70 80 90 100 110 120 VKFQAKLEHE YIQNFKILQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD 130 140 150 160 170 180 GKDYDPVAAR QGQETAVAPS LVAPALNKPK KPLTSSSAAP QRPISTQRTA AAPKAGPGVV 190 200 210 220 230 240 RKNPGVGNGD DEAAELMQQV NVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ 250 260 RIVDILYATD EGFVIPDEGG PQEEQEEY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7606712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH APC.
[2]	"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: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	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, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[5]	"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: 9724749] [Abstract] Cited for: SUBCELLULAR LOCATION.
[6]	"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: 10226031] [Abstract] Cited for: INTERACTION WITH DCTN1; DCTN2 AND DYNEIN INTERMEDIATE CHAIN.
[7]	"EB/RP gene family encodes tubulin binding proteins." Juwana J.-P., Henderikx P., Mischo A., Wadle A., Fadle N., Gerlach K., Arends J.W., Hoogenboom H., Pfreundschuh M., Renner C. Int. J. Cancer 81:275-284(1999) [PubMed: 10188731] [Abstract] Cited for: INTERACTION WITH TUBULIN.
[8]	"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: 10644998] [Abstract] Cited for: INTERACTION WITH APC2, TISSUE SPECIFICITY.
[9]	"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: 11943150] [Abstract] Cited for: INTERACTION WITH TERF1.
[10]	"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: 12388762] [Abstract] Cited for: INTERACTION WITH APC AND DCTN1, SUBCELLULAR LOCATION, FUNCTION.
[11]	"Characterization of functional domains of human EB1 family proteins." Bu W., Su L.-K. J. Biol. Chem. 278:49721-49731(2003) [PubMed: 14514668] [Abstract] Cited for: CHARACTERIZATION, INTERACTION WITH TUBULIN; APC AND DCTN1.
[12]	"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: 15631994] [Abstract] Cited for: INTERACTION WITH CLASP1 AND CLASP2.
[13]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, MASS SPECTROMETRY.
[14]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND THR-166, MASS SPECTROMETRY.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"Structural insights into the EB1-APC interaction." Honnappa S., John C.M., Kostrewa D., Winkler F.K., Steinmetz M.O. EMBO J. 24:261-269(2005) [PubMed: 15616574] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 191-268, DIMERIZATION, INTERACTION WITH APC.
[17]	"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: 12857735] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-130, MUTAGENESIS OF 59-LYS-LYS-60 AND LYS-89.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

U24166 mRNA. Translation: AAC09471.1.
AL035071 Genomic DNA. Translation: CAB53072.1.
BC106068 mRNA. Translation: AAI06069.1.
BC109281 mRNA. Translation: AAI09282.1.

IPI

IPI00017596.

PIR

I52726.

RefSeq

NP_036457.1.

UniGene

Hs.472437

3D structure databases

PDBPDBe

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	185-254	[»]
1YIG	X-ray	2.00	A/B	185-254	[»]
2HKQ	X-ray	1.86	A	191-267	[»]
2HL3	X-ray	2.03	C	263-268	[»]
2HL5	X-ray	1.93	A/B	191-267	[»]
2QJZ	X-ray	1.25	A/B	12-133	[»]
2R8U	X-ray	1.35	A/B	1-268	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15691. 11 interactions.

PTM databases

PhosphoSite

Q15691.

2-D gel databases

OGP

Q15691.

REPRODUCTION-2DPAGE

IPI00017596.

Proteomic databases

PeptideAtlas

Q15691.

PRIDE

Q15691.

Genome annotation databases

Ensembl

ENSG00000101367. Homo sapiens. [Contig view]

GeneID

22919.

KEGG

hsa:22919.

Organism-specific databases

GeneCards

GC20P030871.

H-InvDB

HIX0040584.

HGNC

HGNC:6890. MAPRE1.

HPA

CAB009337.
CAB019391.
HPA003600.

MIM

603108. gene.

PharmGKB

PA30634.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q15691.

HOVERGEN

Q15691.

OMA

Q15691. ISTQRTA.

Enzyme and pathway databases

Reactome

REACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpress

Q15691.

Bgee

Q15691.

CleanEx

HS_MAPRE1.

GermOnline

ENSG00000101367. Homo sapiens.

Family and domain databases

InterPro

IPR001715. Calponin_act_bd.
IPR004953. EB1_C.
[Graphical view]

Pfam

PF00307. CH. 1 hit.
PF03271. EB1. 1 hit.
[Graphical view]

PROSITE

PS50021. CH. 1 hit.
PS51230. EB1_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

43617.

SOURCE

Search...

Entry information

Entry name

MARE1_HUMAN

Accession

Primary (citable) accession number: Q15691
Secondary accession number(s): Q3KQS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)