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Q9UPY8 (MARE3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated protein RP/EB family member 3
Alternative name(s):
EB1 protein family member 3
Short name=EBF3
End-binding protein 3
Short name=EB3
RP3
Gene names
Name:MAPRE3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration By similarity. Ref.16

Subunit structure

Interacts with APC2 By similarity. Homodimer. Heterodimer with MAPRE1. Interacts with DCTN1 and SRCIN1. Binds to the C-terminal domain of APC. Binds monomeric and polymerized tubulin. Interacts (via C-terminus) with CLIP1. Interacts with SLAIN2. Ref.1 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.16

Subcellular location

Cytoplasmcytoskeleton. Note: Associated with the microtubule network. Detected at the plus end of microtubules. Ref.1 Ref.16

Tissue specificity

Predominantly expressed in brain and muscle. Ref.1

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.

Sequence caution

The sequence AAK07556.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAK07557.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA72060.1 differs from that shown. Reason: Frameshift at position 199.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APC2O959967EBI-726739,EBI-1053045
JUNP054123EBI-726739,EBI-852823
Srcin1Q9QWI6-25EBI-726739,EBI-775607From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UPY8-1)

Also known as: EBF3-L;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UPY8-2)

Also known as: EBF3-S;

The sequence of this isoform differs from the canonical sequence as follows:
     142-156: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 281281Microtubule-associated protein RP/EB family member 3
PRO_0000213428

Regions

Domain14 – 116103CH
Domain194 – 26471EB1 C-terminal
Region217 – 28165DCTN1-binding
Region217 – 26044APC-binding

Natural variations

Alternative sequence142 – 15615Missing in isoform 2.
VSP_012947

Experimental info

Sequence conflict21A → P in CAA72060. Ref.7
Sequence conflict131E → V in CAA72060. Ref.7
Sequence conflict1231D → G in CAA72060. Ref.7
Sequence conflict2371C → S in CAG38760. Ref.3

Secondary structure

..................... 281
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (EBF3-L) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 0DA45E89A0B993D3

FASTA28131,982
        10         20         30         40         50         60 
MAVNVYSTSV TSENLSRHDM LAWVNDSLHL NYTKIEQLCS GAAYCQFMDM LFPGCVHLRK 

        70         80         90        100        110        120 
VKFQAKLEHE YIHNFKVLQA AFKKMGVDKI IPVEKLVKGK FQDNFEFIQW FKKFFDANYD 

       130        140        150        160        170        180 
GKDYNPLLAR QGQDVAPPPN PGDQIFNKSK KLIGTAVPQR TSPTGPKNMQ TSGRLSNVAP 

       190        200        210        220        230        240 
PCILRKNPPS ARNGGHETDA QILELNQQLV DLKLTVDGLE KERDFYFSKL RDIELICQEH 

       250        260        270        280 
ESENSPVISG IIGILYATEE GFAPPEDDEI EEHQQEDQDE Y 

« Hide

Isoform 2 (EBF3-S) [UniParc].

Checksum: E66CAD36E28EE645
Show »

FASTA26630,380

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH APC2, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Fetal brain.
[2]"Characterization of human MAPRE genes and their proteins."
Su L.-K., Qi Y.
Genomics 71:142-149(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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].
[6]"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] (ISOFORM 1).
Tissue: Kidney.
[7]"RP1, a new member of the adenomatous polyposis coli-binding EB1-like gene family, is differentially expressed in activated T cells."
Renner C., Pfitzenmeier J.-P., Gerlach K., Held G., Ohnesorge S., Sahin U., Bauer S., Pfreundschuh M.
J. Immunol. 159:1276-1283(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-200 (ISOFORM 1).
[8]"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.
[9]"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.
[10]"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.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity."
Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S., Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J., Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.
Neuron 61:85-100(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRCIN1.
[13]"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].
[14]"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.
[15]"Solution structure of the CH domain of human microtubule-associated protein RP/EB family member 3."
RIKEN structural genomics initiative (RSGI)
Submitted (AUG-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-146.
[16]"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: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-130, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB025186 mRNA. Translation: BAA82958.1.
AF288787 Genomic DNA. Translation: AAK07556.1. Different initiation.
AF288787 Genomic DNA. Translation: AAK07557.1. Different initiation.
CR536523 mRNA. Translation: CAG38760.1.
CR541845 mRNA. Translation: CAG46643.1.
AC013472 Genomic DNA. Translation: AAY14653.1.
CH471053 Genomic DNA. Translation: EAX00660.1.
CH471053 Genomic DNA. Translation: EAX00662.1.
CH471053 Genomic DNA. Translation: EAX00663.1.
CH471053 Genomic DNA. Translation: EAX00666.1.
BC011557 mRNA. Translation: AAH11557.1.
Y11174 mRNA. Translation: CAA72060.1. Frameshift.
RefSeqNP_036458.2. NM_012326.2.
XP_005264271.1. XM_005264214.1.
XP_005264272.1. XM_005264215.1.
XP_005264273.1. XM_005264216.1.
UniGeneHs.515860.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYONMR-A1-146[»]
3CO1X-ray1.40A1-130[»]
3TQ7X-ray2.30B200-281[»]
ProteinModelPortalQ9UPY8.
SMRQ9UPY8. Positions 1-147, 204-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116584. 8 interactions.
DIPDIP-56069N.
IntActQ9UPY8. 12 interactions.
MINTMINT-1417856.
STRING9606.ENSP00000233121.

PTM databases

PhosphoSiteQ9UPY8.

Polymorphism databases

DMDM20138791.

Proteomic databases

PaxDbQ9UPY8.
PRIDEQ9UPY8.

Protocols and materials databases

DNASU22924.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233121; ENSP00000233121; ENSG00000084764. [Q9UPY8-1]
ENST00000402218; ENSP00000385715; ENSG00000084764. [Q9UPY8-2]
ENST00000405074; ENSP00000383915; ENSG00000084764. [Q9UPY8-2]
GeneID22924.
KEGGhsa:22924.
UCSCuc002rhw.3. human. [Q9UPY8-1]

Organism-specific databases

CTD22924.
GeneCardsGC02P027193.
HGNCHGNC:6892. MAPRE3.
HPAHPA009263.
MIM605788. gene.
neXtProtNX_Q9UPY8.
PharmGKBPA30636.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5217.
HOGENOMHOG000198048.
HOVERGENHBG052410.
InParanoidQ9UPY8.
KOK10436.
OMALAWINST.
OrthoDBEOG7ZD1W5.
PhylomeDBQ9UPY8.
TreeFamTF313620.

Gene expression databases

ArrayExpressQ9UPY8.
BgeeQ9UPY8.
CleanExHS_MAPRE3.
GenevestigatorQ9UPY8.

Family and domain databases

Gene3D1.10.418.10. 1 hit.
InterProIPR001715. CH-domain.
IPR004953. EB1_C.
IPR027738. EB3.
IPR027328. MAPRE.
[Graphical view]
PANTHERPTHR10623. PTHR10623. 1 hit.
PTHR10623:SF10. PTHR10623:SF10. 1 hit.
PfamPF00307. CH. 1 hit.
PF03271. EB1. 1 hit.
[Graphical view]
SUPFAMSSF140612. SSF140612. 1 hit.
SSF47576. SSF47576. 1 hit.
PROSITEPS50021. CH. 1 hit.
PS51230. EB1_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UPY8.
GeneWikiMAPRE3.
GenomeRNAi22924.
NextBio43629.
PROQ9UPY8.
SOURCESearch...

Entry information

Entry nameMARE3_HUMAN
AccessionPrimary (citable) accession number: Q9UPY8
Secondary accession number(s): B7WPK5 expand/collapse secondary AC list , O00265, Q6FHB0, Q6FI15, Q9BZP7, Q9BZP8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2000
Last modified: March 19, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM