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Q8BH64 (EHD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
EH domain-containing protein 2
Gene names
Name:Ehd2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in membrane reorganization in response to nucleotide hydrolysis. Binds to liposomes and deforms them into tubules. Plays a role in membrane trafficking between the plasma membrane and endosomes. Important for the internalization of GLUT4. Required for fusion of myoblasts to skeletal muscle myotubes. Required for normal translocation of FER1L5 to the plasma membrane. Binds ATP; does not bind GTP. Ref.1 Ref.5 Ref.7

Enzyme regulation

The very low intrinsic ATPase activity is increased upon interaction with liposomes. Ref.8

Subunit structure

Interacts with EHD1. May also interact with EHD3 and EHD4 By similarity. Interacts with Asn-Pro-Phe (NPF) motifs in target proteins. Homodimer and homooligomer. Interacts with MYOF and EHBP1. Interacts with FER1L5 (via second C2 domain). Ref.1 Ref.5 Ref.7 Ref.8

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein By similarity. Note: Colocalizes with GLUT4 in intracellular tubulovesicular structures that are associated with cortical F-actin. Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes. Ref.1 Ref.5 Ref.8

Tissue specificity

Detected in lung and adipocytes. Detected at lower levels in heart and skeletal muscle. Ref.1

Domain

The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins.

Sequence similarities

Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. EHD subfamily.

Contains 1 dynamin-type G (guanine nucleotide-binding) domain.

Contains 1 EF-hand domain.

Contains 1 EH domain.

Ontologies

Keywords
   Cellular componentCell membrane
Endosome
Membrane
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcortical actin cytoskeleton organization

Inferred from direct assay PubMed 15247266. Source: MGI

endocytic recycling

Inferred from sequence or structural similarity. Source: UniProtKB

endocytosis

Inferred from direct assay Ref.1PubMed 15247266. Source: MGI

positive regulation of endocytic recycling

Inferred from mutant phenotype Ref.7. Source: UniProtKB

positive regulation of myoblast fusion

Inferred from mutant phenotype Ref.7. Source: UniProtKB

protein localization to plasma membrane

Inferred from direct assay Ref.7. Source: UniProtKB

   Cellular_componentcaveola

Inferred from sequence orthology PubMed 24013648. Source: MGI

membrane

Inferred from direct assay Ref.1. Source: MGI

perinuclear region of cytoplasm

Inferred from direct assay PubMed 20489164. Source: MGI

plasma membrane

Inferred from direct assay Ref.7. Source: UniProtKB

recycling endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP binding

Inferred from electronic annotation. Source: InterPro

GTPase activity

Inferred from electronic annotation. Source: InterPro

calcium ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 15247266PubMed 20489164. Source: MGI

protein domain specific binding

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 543543EH domain-containing protein 2
PRO_0000322643

Regions

Domain55 – 286232Dynamin-type G
Domain449 – 53789EH
Domain481 – 51636EF-hand
Nucleotide binding65 – 728ATP
Calcium binding494 – 50512

Sites

Binding site2201ATP
Binding site2581ATP

Amino acid modifications

Modified residue4381Phosphoserine Ref.4 Ref.6
Modified residue4681Phosphoserine By similarity

Experimental info

Mutagenesis651G → R: Inhibits myoblast fusion. Ref.5
Mutagenesis721T → A: Abolishes ATP binding. Ref.8
Mutagenesis941T → A: Abolishes increase of intrinsic ATPase activity upon interaction with membranes. Ref.8
Mutagenesis1571I → Q: Increases intrinsic ATPase activity. Ref.8
Mutagenesis1671R → E: Increases intrinsic ATPase activity. Ref.8
Mutagenesis3221F → A: Abolishes localization at the plasma membrane; reduces increase of intrinsic ATPase activity upon interaction with membranes. Ref.8
Mutagenesis3241K → D: Abolishes localization at the plasma membrane. Ref.8
Mutagenesis3271K → D: Abolishes localization at the plasma membrane; abolishes increase of intrinsic ATPase activity upon interaction with membranes. Ref.8
Mutagenesis3281K → D: Abolishes localization at the plasma membrane; reduces increase of intrinsic ATPase activity upon interaction with membranes. Ref.8
Mutagenesis3291K → D: Abolishes localization at the plasma membrane. Ref.8
Sequence conflict1811R → S in BAC32789. Ref.2

Secondary structure

.............................................................................. 543
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8BH64 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 47637795B0B1096E

FASTA54361,174
        10         20         30         40         50         60 
MFSWLKKGGA RGQRPEAIRT VTSSLKELYR TKLLPLEEHY RFGSFHSPAL EDADFDGKPM 

        70         80         90        100        110        120 
VLVAGQYSTG KTSFIQYLLE QEVPGSRVGP EPTTDCFVAV MHGETEGTVP GNALVVDPEK 

       130        140        150        160        170        180 
PFRKLNPFGN TFLNRFMCAQ LPNQVLESIS IIDTPGILSG AKQRVSRGYD FPAVLRWFAE 

       190        200        210        220        230        240 
RVDLIILLFD AHKLEISDEF SEAIGALRGH EDKIRVVLNK ADMVETQQLM RVYGALMWAL 

       250        260        270        280        290        300 
GKVVGTPEVL RVYIGSFWSQ PLLVPDNRRL FELEEQDLFR DIQGLPRHAA LRKLNDLVKR 

       310        320        330        340        350        360 
ARLVRVHAYI ISYLKKEMPT VFGKENKKKQ LILKLPVIFA KIQLEHHISP GDFPDCQKMQ 

       370        380        390        400        410        420 
ELLMAHDFTK FHSLKPKLLE ALDDMLAQDI AKLMPLLRQE ELESVEAGVQ GGAFEGTRMG 

       430        440        450        460        470        480 
PFVERGPDEA IEDGEEGSED DAEWVVTKDK SKYDEIFYNL APADGKLSGS KAKTWMVGTK 

       490        500        510        520        530        540 
LPNSVLGRIW KLSDVDRDGM LDDEEFALAS HLIEAKLEGH GLPTNLPRRL VPPSKRRQKG 


SAE 

« Hide

References

« Hide 'large scale' references
[1]"EHD2 and the novel EH domain binding protein EHBP1 couple endocytosis to the actin cytoskeleton."
Guilherme A., Soriano N.A., Bose S., Holik J., Bose A., Pomerleau D.P., Furcinitti P., Leszyk J., Corvera S., Czech M.P.
J. Biol. Chem. 279:10593-10605(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EHBP1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
Strain: C57BL/6.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Adipose tissue, Embryonic eye, Embryonic head, Embryonic lung, Forelimb and Liver.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[5]"The endocytic recycling protein EHD2 interacts with myoferlin to regulate myoblast fusion."
Doherty K.R., Demonbreun A.R., Wallace G.Q., Cave A., Posey A.D., Heretis K., Pytel P., McNally E.M.
J. Biol. Chem. 283:20252-20260(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYOF, MUTAGENESIS OF GLY-65, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[7]"Endocytic recycling proteins EHD1 and EHD2 interact with fer-1-like-5 (Fer1L5) and mediate myoblast fusion."
Posey A.D. Jr., Pytel P., Gardikiotes K., Demonbreun A.R., Rainey M., George M., Band H., McNally E.M.
J. Biol. Chem. 286:7379-7388(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FER1L5 AND MYOF.
[8]"Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling."
Daumke O., Lundmark R., Vallis Y., Martens S., Butler P.J.G., McMahon H.T.
Nature 449:923-927(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND CALCIUM IONS, SUBUNIT, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF THR-72; THR-94; ILE-157; ARG-167; PHE-322; LYS-324; LYS-327; LYS-328 AND LYS-329.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY531389 mRNA. Translation: AAS48536.1.
AK031203 mRNA. Translation: BAC27298.1.
AK046566 mRNA. Translation: BAC32789.1.
AK048356 mRNA. Translation: BAC33310.1.
AK050243 mRNA. Translation: BAC34142.1.
AK084455 mRNA. Translation: BAC39188.1.
AK085016 mRNA. Translation: BAC39339.1.
BC113161 mRNA. Translation: AAI13162.1.
CCDSCCDS20842.1.
RefSeqNP_694708.2. NM_153068.3.
UniGeneMm.138215.
Mm.438817.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QPTX-ray3.10A1-543[»]
4CIDX-ray3.00A5-543[»]
ProteinModelPortalQ8BH64.
SMRQ8BH64. Positions 1-539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46806N.
IntActQ8BH64. 2 interactions.

PTM databases

PhosphoSiteQ8BH64.

Proteomic databases

MaxQBQ8BH64.
PaxDbQ8BH64.
PRIDEQ8BH64.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000098799; ENSMUSP00000096397; ENSMUSG00000074364.
GeneID259300.
KEGGmmu:259300.
UCSCuc009fgt.1. mouse.

Organism-specific databases

CTD30846.
MGIMGI:2154274. Ehd2.

Phylogenomic databases

eggNOGNOG136252.
GeneTreeENSGT00700000104190.
HOGENOMHOG000242040.
HOVERGENHBG018183.
InParanoidQ8BH64.
KOK12469.
OMAAPNEGKL.
OrthoDBEOG757CX9.
PhylomeDBQ8BH64.
TreeFamTF314429.

Gene expression databases

ArrayExpressQ8BH64.
BgeeQ8BH64.
CleanExMM_EHD2.
GenevestigatorQ8BH64.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR001401. Dynamin_GTPase.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EPS15_homology.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00350. Dynamin_N. 1 hit.
[Graphical view]
SMARTSM00027. EH. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50031. EH. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8BH64.
NextBio392043.
PROQ8BH64.
SOURCESearch...

Entry information

Entry nameEHD2_MOUSE
AccessionPrimary (citable) accession number: Q8BH64
Secondary accession number(s): Q8BL28
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot