Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

EH domain-containing protein 1

Gene

EHD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. In vitro causes vesiculation of endocytic membranes (PubMed:24019528). Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes (PubMed:15020713, PubMed:17233914, PubMed:20801876). Recruited to endosomal membranes upon nerve growth factor stimulation, indirectly regulates neurite outgrowth (By similarity). Plays a role in myoblast fusion (By similarity). Involved in the unidirectional retrograde dendritic transport of endocytosed BACE1 and in efficient sorting of BACE1 to axons implicating a function in neuronal APP processing (By similarity). Plays a role in the formation of the ciliary vesicle (CV), an early step in cilium biogenesis. Proposed to be required for the fusion of distal appendage vesicles (DAVs) to form the CV by recruiting SNARE complex component SNAP29. Is required for recruitment of transition zone proteins CEP290, RPGRIP1L, TMEM67 and B9D2, and of IFT20 following DAV reorganization before Rab8-dependent ciliary membrane extension. Required for the loss of CCP110 form the mother centriole essential for the maturation of the basal body during ciliogenesis (PubMed:25686250).By similarity5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei220ATPBy similarity1
Binding sitei258ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi65 – 72ATP1 Publication8
Calcium bindingi489 – 500Combined sources1 PublicationAdd BLAST12

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cadherin binding Source: BHF-UCL
  • calcium ion binding Source: InterPro
  • GTP binding Source: InterPro
  • identical protein binding Source: IntAct
  • Rab GTPase binding Source: UniProtKB

GO - Biological processi

  • blood coagulation Source: Reactome
  • cellular response to nerve growth factor stimulus Source: UniProtKB
  • cholesterol homeostasis Source: BHF-UCL
  • cilium assembly Source: UniProtKB
  • endocytic recycling Source: UniProtKB
  • endocytosis Source: UniProtKB
  • intracellular protein transport Source: UniProtKB
  • low-density lipoprotein particle clearance Source: BHF-UCL
  • neuron projection development Source: UniProtKB
  • positive regulation of cholesterol storage Source: BHF-UCL
  • positive regulation of endocytic recycling Source: UniProtKB
  • positive regulation of myoblast fusion Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein localization to cilium Source: UniProtKB

Keywordsi

Biological processCilium biogenesis/degradation, Protein transport, Transport
LigandATP-binding, Calcium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-983231 Factors involved in megakaryocyte development and platelet production

Names & Taxonomyi

Protein namesi
Recommended name:
EH domain-containing protein 1Curated
Alternative name(s):
PAST homolog 11 Publication
Short name:
hPAST11 Publication
TestilinImported
Gene namesi
Name:EHD1Imported
Synonyms:PAST1 Publication, PAST1Imported
ORF Names:CDABP0131
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000110047.17
HGNCiHGNC:3242 EHD1
MIMi605888 gene
neXtProtiNX_Q9H4M9

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi65G → R: Abolishes ATP-binding and localizes to cytoplasm. 1 Publication1
Mutagenesisi203V → P: Greatly reduces oligomerization and interaction with RAB11FIP2. 1 Publication1
Mutagenesisi468K → A: Loss of interaction with MICALL1. 1 Publication1
Mutagenesisi483K → E: Loss of accumulation at the ciliary pocket. Loss of function in ciliogenesis. Loss of association with tubulovesicular structures and altered MICALL1 localization. No effect on MICALL1 localization; when associated with A-485. 2 Publications1
Mutagenesisi485W → A: Loss of accumulation at the ciliary pocket. Loss of function in ciliogenesis. Abolishes interaction with RAB11FIP2. No effect on MICALL1 localization; when associated with E-483. 3 Publications1

Organism-specific databases

DisGeNETi10938
OpenTargetsiENSG00000110047
PharmGKBiPA27677

Polymorphism and mutation databases

BioMutaiEHD1
DMDMi18202945

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001461091 – 534EH domain-containing protein 1Add BLAST534

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei355PhosphoserineCombined sources1
Modified residuei456PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9H4M9
MaxQBiQ9H4M9
PaxDbiQ9H4M9
PeptideAtlasiQ9H4M9
PRIDEiQ9H4M9

PTM databases

iPTMnetiQ9H4M9
PhosphoSitePlusiQ9H4M9
SwissPalmiQ9H4M9

Expressioni

Tissue specificityi

Highly expressed in testis.1 Publication

Gene expression databases

BgeeiENSG00000110047
CleanExiHS_EHD1
ExpressionAtlasiQ9H4M9 baseline and differential
GenevisibleiQ9H4M9 HS

Organism-specific databases

HPAiHPA049890
HPA049986
HPA066751

Interactioni

Subunit structurei

Homooligomer, and heterooligomer with EHD2, EHD3 and EHD4, ATP-binding is required for heterooligomerization (PubMed:16251358, PubMed:17233914, PubMed:18331452). Interacts (via EH domain) with MICALL1 (via NPF1 motif); the interaction is direct and recruits EHD1 to membranes (PubMed:19864458, PubMed:20106972). Interacts with RAB35; the interaction is indirect through MICALL1 and recruits EHD1 to membranes (By similarity). Interacts (via EH domain) with PACSIN2 (via NPF motifs); regulates localization to tubular recycling endosome membranes (PubMed:23596323). Interacts with PACSIN1 (By similarity). Interacts with RAB8A (PubMed:19864458). Interacts with FER1L5 (via second C2 domain) (By similarity). Interacts with MYOF (By similarity). Interacts with ZFYVE20 (PubMed:15020713). Interacts (via EH domain) with RAB11FIP2 (PubMed:16251358).By similarity8 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116138, 75 interactors
IntActiQ9H4M9, 21 interactors
MINTiQ9H4M9
STRINGi9606.ENSP00000320516

Structurei

Secondary structure

1534
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi440 – 443Combined sources4
Helixi445 – 454Combined sources10
Beta strandi458 – 463Combined sources6
Helixi464 – 473Combined sources10
Helixi478 – 488Combined sources11
Beta strandi494 – 497Combined sources4
Helixi498 – 512Combined sources15
Turni523 – 525Combined sources3
Helixi528 – 530Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JQ6NMR-A401-534[»]
2KFFNMR-A435-534[»]
2KFGNMR-A435-534[»]
2KFHNMR-A435-534[»]
2KSPNMR-A435-534[»]
ProteinModelPortaliQ9H4M9
SMRiQ9H4M9
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H4M9

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 286Dynamin-type GPROSITE-ProRule annotationAdd BLAST232
Domaini444 – 532EHPROSITE-ProRule annotationAdd BLAST89
Domaini476 – 511EF-handPROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni65 – 72G1 motifPROSITE-ProRule annotation8
Regioni91 – 92G2 motifPROSITE-ProRule annotation2
Regioni153 – 156G3 motifPROSITE-ProRule annotation4
Regioni219 – 222G4 motifPROSITE-ProRule annotation4
Regioni243G5 motifPROSITE-ProRule annotation1

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili198 – 227Sequence analysisAdd BLAST30

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1954 Eukaryota
ENOG410XYGB LUCA
GeneTreeiENSGT00760000118985
HOGENOMiHOG000242040
HOVERGENiHBG018183
InParanoidiQ9H4M9
KOiK12483
PhylomeDBiQ9H4M9
TreeFamiTF314429

Family and domain databases

InterProiView protein in InterPro
IPR022812 Dynamin_SF
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR000261 EH_dom
IPR031692 EHD_N
IPR030381 G_DYNAMIN_dom
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00350 Dynamin_N, 1 hit
PF12763 EF-hand_4, 1 hit
PF16880 EHD_N, 1 hit
SMARTiView protein in SMART
SM00027 EH, 1 hit
SUPFAMiSSF47473 SSF47473, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 1 hit
PS50222 EF_HAND_2, 1 hit
PS50031 EH, 1 hit
PS51718 G_DYNAMIN_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q9H4M9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSWVSKDAR RKKEPELFQT VAEGLRQLYA QKLLPLEEHY RFHEFHSPAL
60 70 80 90 100
EDADFDNKPM VLLVGQYSTG KTTFIRHLIE QDFPGMRIGP EPTTDSFIAV
110 120 130 140 150
MHGPTEGVVP GNALVVDPRR PFRKLNAFGN AFLNRFMCAQ LPNPVLDSIS
160 170 180 190 200
IIDTPGILSG EKQRISRGYD FAAVLEWFAE RVDRIILLFD AHKLDISDEF
210 220 230 240 250
SEVIKALKNH EDKIRVVLNK ADQIETQQLM RVYGALMWSL GKIINTPEVV
260 270 280 290 300
RVYIGSFWSH PLLIPDNRKL FEAEEQDLFK DIQSLPRNAA LRKLNDLIKR
310 320 330 340 350
ARLAKVHAYI ISSLKKEMPN VFGKESKKKE LVNNLGEIYQ KIEREHQISP
360 370 380 390 400
GDFPSLRKMQ ELLQTQDFSK FQALKPKLLD TVDDMLANDI ARLMVMVRQE
410 420 430 440 450
ESLMPSQVVK GGAFDGTMNG PFGHGYGEGA GEGIDDVEWV VGKDKPTYDE
460 470 480 490 500
IFYTLSPVNG KITGANAKKE MVKSKLPNTV LGKIWKLADV DKDGLLDDEE
510 520 530
FALANHLIKV KLEGHELPAD LPPHLVPPSK RRHE
Length:534
Mass (Da):60,627
Last modified:September 26, 2001 - v2
Checksum:i3330218772A26CE4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti127A → R in AAD45866 (PubMed:10395801).Curated1
Sequence conflicti180 – 182ERV → DCW in AAD45866 (PubMed:10395801).Curated3
Sequence conflicti194L → Q in AAD45866 (PubMed:10395801).Curated1
Sequence conflicti198D → H in AAD45866 (PubMed:10395801).Curated1
Sequence conflicti216V → M in AAD45866 (PubMed:10395801).Curated1
Sequence conflicti435D → H in AAB81204 (PubMed:9253601).Curated1
Sequence conflicti447T → S in AAD45866 (PubMed:10395801).Curated1
Sequence conflicti467A → V in AAD45866 (PubMed:10395801).Curated1
Sequence conflicti480V → E in AAD45866 (PubMed:10395801).Curated1
Sequence conflicti530 – 534KRRHE → SAWGH in AAG02009 (Ref. 3) Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001434 mRNA Translation: AAB81204.1
AF099011 mRNA Translation: AAD45866.1
AY007161 mRNA Translation: AAG02009.1
BC104799 mRNA Translation: AAI04800.1
BC104825 mRNA Translation: AAI04826.1
CCDSiCCDS8084.1
RefSeqiNP_001269373.1, NM_001282444.1
NP_001269374.1, NM_001282445.1
NP_006786.2, NM_006795.3
XP_011543041.1, XM_011544739.1
UniGeneiHs.523774
Hs.708818

Genome annotation databases

EnsembliENST00000320631; ENSP00000320516; ENSG00000110047
ENST00000359393; ENSP00000352354; ENSG00000110047
GeneIDi10938
KEGGihsa:10938
UCSCiuc001obu.3 human

Similar proteinsi

Entry informationi

Entry nameiEHD1_HUMAN
AccessioniPrimary (citable) accession number: Q9H4M9
Secondary accession number(s): O14611, Q2M3Q4, Q9UNR3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: May 23, 2018
This is version 158 of the entry and version 2 of the sequence. See 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, Direct protein sequencing, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health