Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9H4M9 (EHD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 1
Alternative name(s):
PAST homolog 1
Short name=hPAST1
Testilin
Gene names
Name:EHD1
Synonyms:PAST, PAST1
ORF Names:CDABP0131
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Plays a role in myoblast fusion. Recruited to endosomal membranes upon nerve growth factor stimulation, indirectly regulates neurite outgrowth. Ref.6 Ref.8 Ref.14

Subunit structure

Homooligomer, and heterooligomer with EHD2, EHD3 and EHD4. Interacts (via EH domain) with MICALL1 (via NPF1 motif); the interaction is direct and recruits EHD1 to membranes. Interacts with RAB35; the interaction is indirect through MICALL1 and recruits EHD1 to membranes. Interacts (via EH domain) with PACSIN2 (via NPF motifs); regulates localization to tubular recycling endosome membranes. Interacts with PACSIN1. Interacts with RAB8A. Interacts with FER1L5 (via second C2 domain). Interacts with MYOF. Interacts with ZFYVE20. Ref.6 Ref.8 Ref.11 Ref.12 Ref.19

Subcellular location

Recycling endosome membrane; Peripheral membrane protein. Early endosome membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Preferentially associates with tubular recycling endosomes. Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes. Ref.6 Ref.8 Ref.12 Ref.19

Tissue specificity

Highly expressed in testis.

Domain

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

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
   DomainCoiled coil
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cellular response to nerve growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cholesterol homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

endocytic recycling

Inferred from mutant phenotype Ref.6. Source: UniProtKB

endocytosis

Inferred from mutant phenotype Ref.14. Source: UniProtKB

intracellular protein transport

Inferred from mutant phenotype Ref.6. Source: UniProtKB

low-density lipoprotein particle clearance

Inferred from sequence or structural similarity. Source: BHF-UCL

neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cholesterol storage

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of endocytic recycling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of myoblast fusion

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from physical interaction Ref.8. Source: UniProtKB

   Cellular_componentearly endosome membrane

Inferred from direct assay Ref.6. Source: UniProtKB

endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337PubMed 23376485. Source: UniProt

lipid particle

Inferred from sequence or structural similarity. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

platelet dense tubular network membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

recycling endosome membrane

Inferred from direct assay Ref.6Ref.8Ref.12Ref.19. 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

Rab GTPase binding

Inferred from physical interaction Ref.12. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.6Ref.8Ref.12Ref.19. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 534534EH domain-containing protein 1
PRO_0000146109

Regions

Domain55 – 286232Dynamin-type G
Domain444 – 53289EH
Domain476 – 51136EF-hand
Nucleotide binding65 – 728ATP By similarity
Calcium binding489 – 50012
Coiled coil198 – 22730 Potential

Sites

Binding site2201ATP By similarity
Binding site2581ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.18
Modified residue4561Phosphoserine Ref.10 Ref.13 Ref.15 Ref.17

Experimental info

Mutagenesis4681K → A: Loss of interaction with MICALL1. Ref.20
Mutagenesis4831K → E: Loss of association with tubulovesicular structures and altered MICALL1 localization. No effect on MICALL1 localization; when associated with A-485. Ref.12
Mutagenesis4851W → A: No effect on MICALL1 localization; when associated with E-483. Ref.12
Sequence conflict1271A → R in AAD45866. Ref.2
Sequence conflict180 – 1823ERV → DCW in AAD45866. Ref.2
Sequence conflict1941L → Q in AAD45866. Ref.2
Sequence conflict1981D → H in AAD45866. Ref.2
Sequence conflict2161V → M in AAD45866. Ref.2
Sequence conflict4351D → H in AAB81204. Ref.1
Sequence conflict4471T → S in AAD45866. Ref.2
Sequence conflict4671A → V in AAD45866. Ref.2
Sequence conflict4801V → E in AAD45866. Ref.2
Sequence conflict530 – 5345KRRHE → SAWGH in AAG02009. Ref.3

Secondary structure

................. 534
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H4M9 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 3330218772A26CE4

FASTA53460,627
        10         20         30         40         50         60 
MFSWVSKDAR RKKEPELFQT VAEGLRQLYA QKLLPLEEHY RFHEFHSPAL EDADFDNKPM 

        70         80         90        100        110        120 
VLLVGQYSTG KTTFIRHLIE QDFPGMRIGP EPTTDSFIAV MHGPTEGVVP GNALVVDPRR 

       130        140        150        160        170        180 
PFRKLNAFGN AFLNRFMCAQ LPNPVLDSIS IIDTPGILSG EKQRISRGYD FAAVLEWFAE 

       190        200        210        220        230        240 
RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKIRVVLNK ADQIETQQLM RVYGALMWSL 

       250        260        270        280        290        300 
GKIINTPEVV RVYIGSFWSH PLLIPDNRKL FEAEEQDLFK DIQSLPRNAA LRKLNDLIKR 

       310        320        330        340        350        360 
ARLAKVHAYI ISSLKKEMPN VFGKESKKKE LVNNLGEIYQ KIEREHQISP GDFPSLRKMQ 

       370        380        390        400        410        420 
ELLQTQDFSK FQALKPKLLD TVDDMLANDI ARLMVMVRQE ESLMPSQVVK GGAFDGTMNG 

       430        440        450        460        470        480 
PFGHGYGEGA GEGIDDVEWV VGKDKPTYDE IFYTLSPVNG KITGANAKKE MVKSKLPNTV 

       490        500        510        520        530 
LGKIWKLADV DKDGLLDDEE FALANHLIKV KLEGHELPAD LPPHLVPPSK RRHE 

« Hide

References

« Hide 'large scale' references
[1]"A transcript map for the 2.8-Mb region containing the multiple endocrine neoplasia type 1 locus."
Guru S.C., Agarwal S.K., Manickam P., Olufemi S.-E., Crabtree J.S., Weisemann J.M., Kester M.B., Kim Y.S., Wang Y., Emmert-Buck M.R., Liotta L.A., Spiegel A.M., Boguski M.S., Roe B.A., Collins F.S., Burns A.L., Marx S.J., Chandrasekharappa S.C.
Genome Res. 7:725-735(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"EHD1 -- an EH-domain-containing protein with a specific expression pattern."
Mintz L., Galperin E., Pasmanik-Chor M., Tulzinsky S., Bromberg Y., Kozak C.A., Joyner A., Fein A., Horowitz M.
Genomics 59:66-76(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Pediatric leukemia cDNA sequencing project."
Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Leukemia.
[4]"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].
Tissue: Brain.
[5]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10.
Tissue: Platelet.
[6]"Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane."
Naslavsky N., Boehm M., Backlund P.S. Jr., Caplan S.
Mol. Biol. Cell 15:2410-2422(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH ZFYVE20, SUBCELLULAR LOCATION.
[7]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Shared as well as distinct roles of EHD proteins revealed by biochemical and functional comparisons in mammalian cells and C. elegans."
George M., Ying G., Rainey M.A., Solomon A., Parikh P.T., Gao Q., Band V., Band H.
BMC Cell Biol. 8:3-3(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A role for EHD4 in the regulation of early endosomal transport."
Sharma M., Naslavsky N., Caplan S.
Traffic 9:995-1018(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EHD4.
[12]"MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor recycling."
Sharma M., Giridharan S.S., Rahajeng J., Naslavsky N., Caplan S.
Mol. Biol. Cell 20:5181-5194(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MICALL1 AND RAB8A, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-483 AND TRP-485.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Collapsin response mediator protein-2 (Crmp2) regulates trafficking by linking endocytic regulatory proteins to dynein motors."
Rahajeng J., Giridharan S.S., Naslavsky N., Caplan S.
J. Biol. Chem. 285:31918-31922(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOCYTOSIS.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular recycling endosome biogenesis."
Giridharan S.S., Cai B., Vitale N., Naslavsky N., Caplan S.
Mol. Biol. Cell 24:1776-1790(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PACSIN2, SUBCELLULAR LOCATION.
[20]"Mechanism for the selective interaction of C-terminal Eps15 homology domain proteins with specific Asn-Pro-Phe-containing partners."
Kieken F., Sharma M., Jovic M., Giridharan S.S., Naslavsky N., Caplan S., Sorgen P.L.
J. Biol. Chem. 285:8687-8694(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 435-534 IN COMPLEX WITH MICALL1 PEPTIDE, MUTAGENESIS OF LYS-468.
[21]"EH domain of EHD1."
Kieken F., Jovic M., Naslavsky N., Caplan S., Sorgen P.L.
J. Biomol. NMR 39:323-329(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 401-534 IN COMPLEX WITH CALCIUM IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS8084.1.
RefSeqNP_001269373.1. NM_001282444.1.
NP_001269374.1. NM_001282445.1.
NP_006786.2. NM_006795.3.
XP_006718487.1. XM_006718424.1.
UniGeneHs.523774.
Hs.708818.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JQ6NMR-A401-534[»]
2KFFNMR-A435-534[»]
2KFGNMR-A435-534[»]
2KFHNMR-A435-534[»]
2KSPNMR-A435-534[»]
ProteinModelPortalQ9H4M9.
SMRQ9H4M9. Positions 19-534.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116138. 41 interactions.
IntActQ9H4M9. 4 interactions.
MINTMINT-4999249.
STRING9606.ENSP00000320516.

PTM databases

PhosphoSiteQ9H4M9.

Polymorphism databases

DMDM18202945.

Proteomic databases

MaxQBQ9H4M9.
PaxDbQ9H4M9.
PeptideAtlasQ9H4M9.
PRIDEQ9H4M9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320631; ENSP00000320516; ENSG00000110047.
ENST00000359393; ENSP00000352354; ENSG00000110047.
GeneID10938.
KEGGhsa:10938.
UCSCuc001obu.1. human.

Organism-specific databases

CTD10938.
GeneCardsGC11M064619.
H-InvDBHIX0171322.
HGNCHGNC:3242. EHD1.
MIM605888. gene.
neXtProtNX_Q9H4M9.
PharmGKBPA27677.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG136252.
HOGENOMHOG000242040.
HOVERGENHBG018183.
InParanoidQ9H4M9.
KOK12483.
OMAQAYIISS.
OrthoDBEOG757CX9.
PhylomeDBQ9H4M9.
TreeFamTF314429.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ9H4M9.
BgeeQ9H4M9.
CleanExHS_EHD1.
GenevestigatorQ9H4M9.

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

EvolutionaryTraceQ9H4M9.
GeneWikiEHD1.
GenomeRNAi10938.
NextBio41547.
PROQ9H4M9.
SOURCESearch...

Entry information

Entry nameEHD1_HUMAN
AccessionPrimary (citable) accession number: Q9H4M9
Secondary accession number(s): O14611, Q2M3Q4, Q9UNR3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM