Q15691 (MARE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	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. Ref.12 Ref.22 Ref.25 Ref.28
Subunit structure	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 (via C-terminus) with CLIP1. Interacts with SLAIN2. Interacts with KIF18B; this interaction is required for efficient accumulation of KIF18B at microtubule plus ends. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.25 Ref.28
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Note: Associated with the microtubule network at the growing distal tip of microtubules. Also enriched at the centrosome. Ref.7 Ref.12 Ref.22 Ref.25 Ref.28
Tissue specificity	Ubiquitously expressed. Ref.10
Domain	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 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 Cytoskeleton Microtubule
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Traceable author statement Ref.1. Source: ProtInc mitotic prometaphase Traceable author statement. Source: Reactome negative regulation of microtubule polymerization Inferred from direct assay Ref.11. Source: UniProtKB protein localization to microtubule Inferred from direct assay Ref.28. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara cell projection membrane Inferred from electronic annotation. Source: Compara centrosome Inferred from direct assay PubMed 21399614. Source: UniProtKB cortical microtubule cytoskeleton Inferred from direct assay Ref.14. Source: UniProtKB cytoplasmic microtubule Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome microtubule Inferred from direct assay PubMed 10773885. Source: UniProtKB microtubule plus end Inferred from electronic annotation. Source: Compara
Molecular_function	microtubule plus-end binding Inferred from direct assay Ref.14Ref.28. Source: UniProtKB protein C-terminus binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APC	P25054	4	EBI-1004115,EBI-727707
DST	Q03001	2	EBI-1004115,EBI-310758
TERF1	P54274	2	EBI-1004115,EBI-710997

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

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

124 – 268

145

Interaction with MTUS2/TIP150

Region

185 – 268

84

Interaction with CDK5RAP2

Region

208 – 268

61

DCTN1-binding

Region

220 – 242

23

APC-binding

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Modified residue

124

1

Phosphotyrosine Ref.15

Experimental info

Mutagenesis

59 – 60

2

KK → EE: No effect.

Mutagenesis

89

1

K → E: Loss of binding to microtubules. Ref.24

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

Turn

97 – 99

3

Helix

101 – 118

18

Helix

126 – 129

4

Helix

192 – 230

39

Turn

231 – 233

3

Helix

237 – 247

11

Beta strand

250 – 252

3

Sequences

	Sequence		Length	Mass (Da)
	Q15691 [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] [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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, 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]	"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] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
[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]	"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.
[18]	"Mammalian end binding proteins control persistent microtubule growth." Komarova Y., De Groot C.O., Grigoriev I., Gouveia S.M., Munteanu E.L., Schober J.M., Honnappa S., Buey R.M., Hoogenraad C.C., Dogterom M., Borisy G.G., Steinmetz M.O., Akhmanova A. J. Cell Biol. 184:691-706(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAPRE3.
[19]	"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.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"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.
[22]	"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.
[23]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 191-268, DIMERIZATION, INTERACTION WITH APC.
[24]	"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.
[25]	"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.
[26]	"Key interaction modes of dynamic +TIP networks." Honnappa S., Okhrimenko O., Jaussi R., Jawhari H., Jelesarov I., Winkler F.K., Steinmetz M.O. Mol. Cell 23:663-671(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 191-267 IN COMPLEX WITH DCTN1.
[27]	"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.
[28]	"An EB1-binding motif acts as a microtubule tip localization signal." Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S., Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A., Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O. Cell 138:366-376(2009) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00017596.

PIR

I52726.

RefSeq

NP_036457.1. NM_012325.2.

UniGene

Hs.472437.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3GJO	X-ray	2.50	A/B/C/D	191-260	[»]
3TQ7	X-ray	2.30	A	191-268	[»]

ProteinModelPortal

Q15691.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38018N.

IntAct

Q15691. 15 interactions.

MINT

MINT-206298.

STRING

9606.ENSP00000364721.

PTM databases

PhosphoSite

Q15691.

Polymorphism databases

DMDM

20138589.

2D gel databases

OGP

Q15691.

REPRODUCTION-2DPAGE

IPI00017596.

Proteomic databases

PaxDb

Q15691.

PeptideAtlas

Q15691.

PRIDE

Q15691.

Protocols and materials databases

DNASU

22919.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375571; ENSP00000364721; ENSG00000101367.

GeneID

22919.

KEGG

hsa:22919.

UCSC

uc002wyh.3. human.

Organism-specific databases

CTD

22919.

GeneCards

GC20P031407.

HGNC

HGNC:6890. MAPRE1.

HPA

CAB009337.
CAB019391.
HPA003600.

MIM

603108. gene.

neXtProt

NX_Q15691.

PharmGKB

PA30634.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5217.

HOGENOM

HOG000198048.

HOVERGEN

HBG052410.

InParanoid

Q15691.

KO

K10436.

OMA

ATPPNRM.

OrthoDB

EOG41ZFBH.

PhylomeDB

Q15691.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

Bgee

Q15691.

CleanEx

HS_MAPRE1.

Genevestigator

Q15691.

GermOnline

ENSG00000101367. Homo sapiens.

Family and domain databases

Gene3D

1.10.418.10. 1 hit.

InterPro

IPR001715. CH-domain.
IPR004953. EB1_C.
IPR027328. MAPRE.
[Graphical view]

PANTHER

PTHR10623. PTHR10623. 1 hit.

Pfam

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

SUPFAM

SSF47576. Calponin-homology. 1 hit.
SSF140612. SSF140612. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

ChiTaRS

MAPRE1. human.

EvolutionaryTrace

Q15691.

GenomeRNAi

22919.

NextBio

43617.

SOURCE

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Entry information

Entry name

MARE1_HUMAN

Accession

Primary (citable) accession number: Q15691
Secondary accession number(s): B2R6I7, E1P5M8, Q3KQS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 139 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.