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Protein

EH domain-containing protein 1

Gene

EHD1

Organism
Homo sapiens (Human)
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. 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 involved in cell-cell adhesion Source: BHF-UCL
  • calcium ion binding Source: InterPro
  • GTP binding Source: InterPro
  • 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
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Protein transport, Transport

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110047-MONOMER.
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

HGNCiHGNC:3242. EHD1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • ciliary pocket membrane Source: UniProtKB
  • early endosome membrane Source: UniProtKB
  • endosome membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • lipid particle Source: BHF-UCL
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • platelet dense tubular network membrane Source: BHF-UCL
  • recycling endosome membrane Source: UniProtKB
Complete GO annotation...

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.

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

WithEntry#Exp.IntActNotes
ANKFY1Q9P2R38EBI-490691,EBI-2513908
Ehd3Q9QXY67EBI-490691,EBI-775304From a different organism.
MICALL1Q8N3F812EBI-490691,EBI-1056885
RBSNE1B9V62EBI-490691,EBI-12509611From a different organism.
RBSNQ9H1K03EBI-490691,EBI-1105310

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116138. 69 interactors.
IntActiQ9H4M9. 18 interactors.
MINTiMINT-4999249.
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 GAdd BLAST232
Domaini444 – 532EHPROSITE-ProRule annotationAdd BLAST89
Domaini476 – 511EF-handPROSITE-ProRule annotationAdd BLAST36

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

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1954. Eukaryota.
ENOG410XYGB. LUCA.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000242040.
HOVERGENiHBG018183.
InParanoidiQ9H4M9.
KOiK12483.
PhylomeDBiQ9H4M9.
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.
IPR029951. EHD1/EHD3.
IPR031692. EHD_N.
IPR030381. G_DYNAMIN_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11216:SF67. PTHR11216:SF67. 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.

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi116138. 69 interactors.
IntActiQ9H4M9. 18 interactors.
MINTiMINT-4999249.
STRINGi9606.ENSP00000320516.

PTM databases

iPTMnetiQ9H4M9.
PhosphoSitePlusiQ9H4M9.
SwissPalmiQ9H4M9.

Polymorphism and mutation databases

BioMutaiEHD1.
DMDMi18202945.

Proteomic databases

EPDiQ9H4M9.
MaxQBiQ9H4M9.
PaxDbiQ9H4M9.
PeptideAtlasiQ9H4M9.
PRIDEiQ9H4M9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10938.
DisGeNETi10938.
GeneCardsiEHD1.
H-InvDBHIX0171322.
HGNCiHGNC:3242. EHD1.
HPAiHPA049890.
HPA049986.
MIMi605888. gene.
neXtProtiNX_Q9H4M9.
OpenTargetsiENSG00000110047.
PharmGKBiPA27677.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1954. Eukaryota.
ENOG410XYGB. LUCA.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000242040.
HOVERGENiHBG018183.
InParanoidiQ9H4M9.
KOiK12483.
PhylomeDBiQ9H4M9.
TreeFamiTF314429.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110047-MONOMER.
ReactomeiR-HSA-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiEHD1. human.
EvolutionaryTraceiQ9H4M9.
GeneWikiiEHD1.
GenomeRNAii10938.
PROiQ9H4M9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000110047.
CleanExiHS_EHD1.
ExpressionAtlasiQ9H4M9. baseline and differential.
GenevisibleiQ9H4M9. HS.

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.
IPR029951. EHD1/EHD3.
IPR031692. EHD_N.
IPR030381. G_DYNAMIN_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11216:SF67. PTHR11216:SF67. 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 nameiEHD1_HUMAN
AccessioniPrimary (citable) accession number: Q9H4M9
Secondary accession number(s): O14611, Q2M3Q4, Q9UNR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: November 30, 2016
This is version 147 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

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.