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Q9UPY8

- MARE3_HUMAN

UniProt

Q9UPY8 - MARE3_HUMAN

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Protein

Microtubule-associated protein RP/EB family member 3

Gene

MAPRE3

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 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).By similarity

GO - Molecular functioni

  1. microtubule binding Source: BHF-UCL

GO - Biological processi

  1. mitotic nuclear division Source: UniProtKB-KW
  2. positive regulation of cyclin-dependent protein serine/threonine kinase activity Source: BHF-UCL
  3. positive regulation of microtubule plus-end binding Source: Ensembl
  4. positive regulation of transcription, DNA-templated Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MAPRE3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6892. MAPRE3.

Subcellular locationi

Cytoplasmcytoskeleton 2 Publications
Note: Associated with the microtubule network. Detected at the plus end of microtubules.

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. microtubule cytoskeleton Source: BHF-UCL
  3. microtubule plus-end Source: Ensembl
  4. midbody Source: BHF-UCL
  5. perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30636.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281Microtubule-associated protein RP/EB family member 3PRO_0000213428Add
BLAST

Proteomic databases

MaxQBiQ9UPY8.
PaxDbiQ9UPY8.
PRIDEiQ9UPY8.

PTM databases

PhosphoSiteiQ9UPY8.

Expressioni

Tissue specificityi

Predominantly expressed in brain and muscle.1 Publication

Gene expression databases

BgeeiQ9UPY8.
CleanExiHS_MAPRE3.
ExpressionAtlasiQ9UPY8. baseline and differential.
GenevestigatoriQ9UPY8.

Organism-specific databases

HPAiHPA009263.

Interactioni

Subunit structurei

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.By similarity7 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi116584. 10 interactions.
DIPiDIP-56069N.
IntActiQ9UPY8. 12 interactions.
MINTiMINT-1417856.
STRINGi9606.ENSP00000233121.

Structurei

Secondary structure

1
281
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 2812Combined sources
Helixi35 – 406Combined sources
Helixi42 – 5110Combined sources
Helixi58 – 603Combined sources
Helixi68 – 8518Combined sources
Helixi93 – 975Combined sources
Helixi101 – 11818Combined sources
Turni126 – 1294Combined sources
Helixi206 – 23833Combined sources
Helixi247 – 2559Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYONMR-A1-146[»]
3CO1X-ray1.40A1-130[»]
3TQ7X-ray2.30B200-281[»]
ProteinModelPortaliQ9UPY8.
SMRiQ9UPY8. Positions 1-147, 204-260.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UPY8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 116103CHPROSITE-ProRule annotationAdd
BLAST
Domaini194 – 26471EB1 C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni217 – 28165DCTN1-bindingAdd
BLAST
Regioni217 – 26044APC-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.
InParanoidiQ9UPY8.
KOiK10436.
OMAiNYHALER.
OrthoDBiEOG7ZD1W5.
PhylomeDBiQ9UPY8.
TreeFamiTF313620.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR004953. EB1_C.
IPR027738. EB3_vertebrate.
IPR027328. MAPRE.
[Graphical view]
PANTHERiPTHR10623. PTHR10623. 1 hit.
PTHR10623:SF10. PTHR10623:SF10. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UPY8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAVNVYSTSV TSENLSRHDM LAWVNDSLHL NYTKIEQLCS GAAYCQFMDM
60 70 80 90 100
LFPGCVHLRK VKFQAKLEHE YIHNFKVLQA AFKKMGVDKI IPVEKLVKGK
110 120 130 140 150
FQDNFEFIQW FKKFFDANYD GKDYNPLLAR QGQDVAPPPN PGDQIFNKSK
160 170 180 190 200
KLIGTAVPQR TSPTGPKNMQ TSGRLSNVAP PCILRKNPPS ARNGGHETDA
210 220 230 240 250
QILELNQQLV DLKLTVDGLE KERDFYFSKL RDIELICQEH ESENSPVISG
260 270 280
IIGILYATEE GFAPPEDDEI EEHQQEDQDE Y
Length:281
Mass (Da):31,982
Last modified:May 1, 2000 - v1
Checksum:i0DA45E89A0B993D3
GO
Isoform 2 (identifier: Q9UPY8-2) [UniParc]FASTAAdd to Basket

Also known as: EBF3-S

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

Show »
Length:266
Mass (Da):30,380
Checksum:iE66CAD36E28EE645
GO

Sequence cautioni

The sequence AAK07556.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAK07557.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA72060.1 differs from that shown. Reason: Frameshift at position 199. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → P in CAA72060. (PubMed:9233623)Curated
Sequence conflicti13 – 131E → V in CAA72060. (PubMed:9233623)Curated
Sequence conflicti123 – 1231D → G in CAA72060. (PubMed:9233623)Curated
Sequence conflicti237 – 2371C → S in CAG38760. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei142 – 15615Missing in isoform 2. 1 PublicationVSP_012947Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1731.1. [Q9UPY8-1]
RefSeqiNP_036458.2. NM_012326.2. [Q9UPY8-1]
XP_006712030.1. XM_006711967.1. [Q9UPY8-2]
UniGeneiHs.515860.

Genome annotation databases

EnsembliENST00000233121; ENSP00000233121; ENSG00000084764. [Q9UPY8-1]
ENST00000402218; ENSP00000385715; ENSG00000084764. [Q9UPY8-2]
ENST00000405074; ENSP00000383915; ENSG00000084764. [Q9UPY8-2]
GeneIDi22924.
KEGGihsa:22924.
UCSCiuc002rhw.3. human. [Q9UPY8-1]

Polymorphism databases

DMDMi20138791.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS1731.1. [Q9UPY8-1 ]
RefSeqi NP_036458.2. NM_012326.2. [Q9UPY8-1 ]
XP_006712030.1. XM_006711967.1. [Q9UPY8-2 ]
UniGenei Hs.515860.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WYO NMR - A 1-146 [» ]
3CO1 X-ray 1.40 A 1-130 [» ]
3TQ7 X-ray 2.30 B 200-281 [» ]
ProteinModelPortali Q9UPY8.
SMRi Q9UPY8. Positions 1-147, 204-260.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116584. 10 interactions.
DIPi DIP-56069N.
IntActi Q9UPY8. 12 interactions.
MINTi MINT-1417856.
STRINGi 9606.ENSP00000233121.

PTM databases

PhosphoSitei Q9UPY8.

Polymorphism databases

DMDMi 20138791.

Proteomic databases

MaxQBi Q9UPY8.
PaxDbi Q9UPY8.
PRIDEi Q9UPY8.

Protocols and materials databases

DNASUi 22924.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000233121 ; ENSP00000233121 ; ENSG00000084764 . [Q9UPY8-1 ]
ENST00000402218 ; ENSP00000385715 ; ENSG00000084764 . [Q9UPY8-2 ]
ENST00000405074 ; ENSP00000383915 ; ENSG00000084764 . [Q9UPY8-2 ]
GeneIDi 22924.
KEGGi hsa:22924.
UCSCi uc002rhw.3. human. [Q9UPY8-1 ]

Organism-specific databases

CTDi 22924.
GeneCardsi GC02P027193.
HGNCi HGNC:6892. MAPRE3.
HPAi HPA009263.
MIMi 605788. gene.
neXtProti NX_Q9UPY8.
PharmGKBi PA30636.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5217.
GeneTreei ENSGT00490000043329.
HOGENOMi HOG000198048.
HOVERGENi HBG052410.
InParanoidi Q9UPY8.
KOi K10436.
OMAi NYHALER.
OrthoDBi EOG7ZD1W5.
PhylomeDBi Q9UPY8.
TreeFami TF313620.

Miscellaneous databases

ChiTaRSi MAPRE3. human.
EvolutionaryTracei Q9UPY8.
GeneWikii MAPRE3.
GenomeRNAii 22924.
NextBioi 43629.
PROi Q9UPY8.
SOURCEi Search...

Gene expression databases

Bgeei Q9UPY8.
CleanExi HS_MAPRE3.
ExpressionAtlasi Q9UPY8. baseline and differential.
Genevestigatori Q9UPY8.

Family and domain databases

Gene3Di 1.10.418.10. 1 hit.
InterProi IPR001715. CH-domain.
IPR004953. EB1_C.
IPR027738. EB3_vertebrate.
IPR027328. MAPRE.
[Graphical view ]
PANTHERi PTHR10623. PTHR10623. 1 hit.
PTHR10623:SF10. PTHR10623:SF10. 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. "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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: INTERACTION WITH SRCIN1.
  13. 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. Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-130, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiMARE3_HUMAN
AccessioniPrimary (citable) accession number: Q9UPY8
Secondary accession number(s): B7WPK5
, O00265, Q6FHB0, Q6FI15, Q9BZP7, Q9BZP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 133 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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