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Protein

EH domain-containing protein 2

Gene

Ehd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis (PubMed:24508342). Plays a role in membrane trafficking between the plasma membrane and endosomes. Important for the internalization of GLUT4 (PubMed:14676205). Required for fusion of myoblasts to skeletal muscle myotubes. Required for normal translocation of FER1L5 to the plasma membrane (PubMed:18502764, PubMed:21177873).4 Publications

Enzyme regulationi

The very low intrinsic ATPase activity is increased upon interaction with liposomes.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei220ATPCombined sources1 Publication1
Binding sitei258ATPCombined sources2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi65 – 72ATPCombined sources2 Publications8
Calcium bindingi494 – 505Combined sources2 PublicationsAdd BLAST12

GO - Molecular functioni

GO - Biological processi

  • cortical actin cytoskeleton organization Source: MGI
  • endocytic recycling Source: UniProtKB
  • endocytosis Source: MGI
  • membrane tubulation Source: UniProtKB
  • positive regulation of endocytic recycling Source: UniProtKB
  • positive regulation of myoblast fusion Source: UniProtKB
  • protein localization to plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
EH domain-containing protein 2Curated
Gene namesi
Name:Ehd2Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2154274. Ehd2.

Subcellular locationi

GO - Cellular componenti

  • caveola Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: MGI
  • extrinsic component of membrane Source: UniProtKB
  • membrane Source: MGI
  • perinuclear region of cytoplasm Source: MGI
  • plasma membrane Source: UniProtKB
  • recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi65G → R: Inhibits myoblast fusion. 1 Publication1
Mutagenesisi72T → A: Abolishes ATP binding. 1 Publication1
Mutagenesisi94T → A: Abolishes increase of intrinsic ATPase activity upon interaction with membranes. 1 Publication1
Mutagenesisi157I → Q: Increases intrinsic ATPase activity. 1 Publication1
Mutagenesisi167R → E: Increases intrinsic ATPase activity. 1 Publication1
Mutagenesisi322F → A: Abolishes localization at the plasma membrane; reduces increase of intrinsic ATPase activity upon interaction with membranes. 1 Publication1
Mutagenesisi324K → D: Abolishes localization at the plasma membrane. 1 Publication1
Mutagenesisi327K → D: Abolishes localization at the plasma membrane; abolishes increase of intrinsic ATPase activity upon interaction with membranes. 1 Publication1
Mutagenesisi328K → D: Abolishes localization at the plasma membrane; reduces increase of intrinsic ATPase activity upon interaction with membranes. 1 Publication1
Mutagenesisi329K → D: Abolishes localization at the plasma membrane. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003226431 – 543EH domain-containing protein 2Add BLAST543

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3PhosphoserineBy similarity1
Modified residuei44PhosphoserineCombined sources1
Modified residuei438PhosphoserineCombined sources1
Modified residuei468PhosphoserineCombined sources1
Modified residuei470PhosphoserineBy similarity1
Modified residuei484PhosphoserineBy similarity1
Modified residuei493PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BH64.
MaxQBiQ8BH64.
PaxDbiQ8BH64.
PeptideAtlasiQ8BH64.
PRIDEiQ8BH64.

PTM databases

iPTMnetiQ8BH64.
PhosphoSitePlusiQ8BH64.
SwissPalmiQ8BH64.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000074364.
CleanExiMM_EHD2.
ExpressionAtlasiQ8BH64. baseline and differential.
GenevisibleiQ8BH64. MM.

Interactioni

Subunit structurei

Homodimer and homooligomer (By similarity). Interacts with EHD1 (By similarity). May also interact with EHD3 and EHD4 (By similarity). Interacts with MYOF (PubMed:18502764, PubMed:21177873). Interacts with EHBP1 (PubMed:14676205). Interacts with FER1L5 (via second C2 domain) (PubMed:21177873).By similarity4 Publications

GO - Molecular functioni

  • protein domain specific binding Source: MGI

Protein-protein interaction databases

DIPiDIP-46806N.
IntActiQ8BH64. 3 interactors.
STRINGi10090.ENSMUSP00000096397.

Structurei

Secondary structure

1543
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 32Combined sources12
Helixi34 – 39Combined sources6
Helixi42 – 44Combined sources3
Helixi52 – 56Combined sources5
Beta strandi60 – 66Combined sources7
Helixi71 – 79Combined sources9
Beta strandi96 – 102Combined sources7
Beta strandi104 – 109Combined sources6
Beta strandi134 – 141Combined sources8
Helixi145 – 147Combined sources3
Beta strandi150 – 153Combined sources4
Helixi171 – 181Combined sources11
Beta strandi183 – 190Combined sources8
Helixi191 – 193Combined sources3
Helixi198 – 207Combined sources10
Helixi211 – 213Combined sources3
Beta strandi214 – 219Combined sources6
Turni220 – 223Combined sources4
Helixi226 – 244Combined sources19
Beta strandi252 – 255Combined sources4
Beta strandi258 – 260Combined sources3
Helixi268 – 283Combined sources16
Turni284 – 288Combined sources5
Helixi289 – 317Combined sources29
Beta strandi320 – 323Combined sources4
Helixi324 – 346Combined sources23
Helixi350 – 352Combined sources3
Helixi356 – 364Combined sources9
Helixi368 – 370Combined sources3
Helixi376 – 387Combined sources12
Helixi389 – 403Combined sources15
Helixi405 – 407Combined sources3
Beta strandi411 – 414Combined sources4
Helixi416 – 419Combined sources4
Helixi447 – 459Combined sources13
Beta strandi466 – 468Combined sources3
Helixi469 – 476Combined sources8
Helixi477 – 479Combined sources3
Helixi483 – 493Combined sources11
Beta strandi498 – 502Combined sources5
Helixi503 – 518Combined sources16
Helixi528 – 530Combined sources3
Helixi533 – 535Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QPTX-ray3.10A1-543[»]
4CIDX-ray3.00A5-543[»]
ProteinModelPortaliQ8BH64.
SMRiQ8BH64.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8BH64.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 286Dynamin-type GAdd BLAST232
Domaini449 – 537EHPROSITE-ProRule annotationAdd BLAST89
Domaini481 – 516EF-handPROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni320 – 340Mediates membrane-binding1 PublicationAdd BLAST21

Domaini

The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins.1 Publication

Sequence similaritiesi

Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 1 EH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1954. Eukaryota.
ENOG410XYGB. LUCA.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000242040.
HOVERGENiHBG018183.
InParanoidiQ8BH64.
KOiK12469.
OMAiMQEMLMA.
OrthoDBiEOG091G04KA.
PhylomeDBiQ8BH64.
TreeFamiTF314429.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR022812. Dynamin_SF.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EH_dom.
IPR029945. EHD2.
IPR031692. EHD_N.
IPR030381. G_DYNAMIN_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11216:SF62. PTHR11216:SF62. 1 hit.
PfamiPF00350. Dynamin_N. 1 hit.
PF12763. EF-hand_4. 1 hit.
PF16880. EHD_N. 1 hit.
[Graphical view]
SMARTiSM00027. EH. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50031. EH. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BH64-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSWLKKGGA RGQRPEAIRT VTSSLKELYR TKLLPLEEHY RFGSFHSPAL
60 70 80 90 100
EDADFDGKPM VLVAGQYSTG KTSFIQYLLE QEVPGSRVGP EPTTDCFVAV
110 120 130 140 150
MHGETEGTVP GNALVVDPEK PFRKLNPFGN TFLNRFMCAQ LPNQVLESIS
160 170 180 190 200
IIDTPGILSG AKQRVSRGYD FPAVLRWFAE RVDLIILLFD AHKLEISDEF
210 220 230 240 250
SEAIGALRGH EDKIRVVLNK ADMVETQQLM RVYGALMWAL GKVVGTPEVL
260 270 280 290 300
RVYIGSFWSQ PLLVPDNRRL FELEEQDLFR DIQGLPRHAA LRKLNDLVKR
310 320 330 340 350
ARLVRVHAYI ISYLKKEMPT VFGKENKKKQ LILKLPVIFA KIQLEHHISP
360 370 380 390 400
GDFPDCQKMQ ELLMAHDFTK FHSLKPKLLE ALDDMLAQDI AKLMPLLRQE
410 420 430 440 450
ELESVEAGVQ GGAFEGTRMG PFVERGPDEA IEDGEEGSED DAEWVVTKDK
460 470 480 490 500
SKYDEIFYNL APADGKLSGS KAKTWMVGTK LPNSVLGRIW KLSDVDRDGM
510 520 530 540
LDDEEFALAS HLIEAKLEGH GLPTNLPRRL VPPSKRRQKG SAE
Length:543
Mass (Da):61,174
Last modified:March 1, 2003 - v1
Checksum:i47637795B0B1096E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti181R → S in BAC32789 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS20842.1.
RefSeqiNP_694708.2. NM_153068.3.
XP_011248884.1. XM_011250582.2.
UniGeneiMm.138215.
Mm.438817.

Genome annotation databases

EnsembliENSMUST00000098799; ENSMUSP00000096397; ENSMUSG00000074364.
GeneIDi259300.
KEGGimmu:259300.
UCSCiuc009fgt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS20842.1.
RefSeqiNP_694708.2. NM_153068.3.
XP_011248884.1. XM_011250582.2.
UniGeneiMm.138215.
Mm.438817.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QPTX-ray3.10A1-543[»]
4CIDX-ray3.00A5-543[»]
ProteinModelPortaliQ8BH64.
SMRiQ8BH64.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46806N.
IntActiQ8BH64. 3 interactors.
STRINGi10090.ENSMUSP00000096397.

PTM databases

iPTMnetiQ8BH64.
PhosphoSitePlusiQ8BH64.
SwissPalmiQ8BH64.

Proteomic databases

EPDiQ8BH64.
MaxQBiQ8BH64.
PaxDbiQ8BH64.
PeptideAtlasiQ8BH64.
PRIDEiQ8BH64.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098799; ENSMUSP00000096397; ENSMUSG00000074364.
GeneIDi259300.
KEGGimmu:259300.
UCSCiuc009fgt.1. mouse.

Organism-specific databases

CTDi30846.
MGIiMGI:2154274. Ehd2.

Phylogenomic databases

eggNOGiKOG1954. Eukaryota.
ENOG410XYGB. LUCA.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000242040.
HOVERGENiHBG018183.
InParanoidiQ8BH64.
KOiK12469.
OMAiMQEMLMA.
OrthoDBiEOG091G04KA.
PhylomeDBiQ8BH64.
TreeFamiTF314429.

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTraceiQ8BH64.
PROiQ8BH64.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000074364.
CleanExiMM_EHD2.
ExpressionAtlasiQ8BH64. baseline and differential.
GenevisibleiQ8BH64. MM.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR022812. Dynamin_SF.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EH_dom.
IPR029945. EHD2.
IPR031692. EHD_N.
IPR030381. G_DYNAMIN_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11216:SF62. PTHR11216:SF62. 1 hit.
PfamiPF00350. Dynamin_N. 1 hit.
PF12763. EF-hand_4. 1 hit.
PF16880. EHD_N. 1 hit.
[Graphical view]
SMARTiSM00027. EH. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50031. EH. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEHD2_MOUSE
AccessioniPrimary (citable) accession number: Q8BH64
Secondary accession number(s): Q8BL28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 1, 2003
Last modified: November 30, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.