EHD1_HUMAN
ID EHD1_HUMAN Reviewed; 534 AA.
AC Q9H4M9; O14611; Q2M3Q4; Q9UNR3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=EH domain-containing protein 1 {ECO:0000305};
DE AltName: Full=PAST homolog 1 {ECO:0000303|PubMed:9253601};
DE Short=hPAST1 {ECO:0000303|PubMed:9253601};
DE AltName: Full=Testilin {ECO:0000312|EMBL:AAD45866.1};
GN Name=EHD1 {ECO:0000312|HGNC:HGNC:3242};
GN Synonyms=PAST {ECO:0000303|PubMed:9253601},
GN PAST1 {ECO:0000312|HGNC:HGNC:3242}; ORFNames=CDABP0131;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9253601; DOI=10.1101/gr.7.7.725;
RA Guru S.C., Agarwal S.K., Manickam P., Olufemi S.-E., Crabtree J.S.,
RA Weisemann J.M., Kester M.B., Kim Y.S., Wang Y., Emmert-Buck M.R.,
RA Liotta L.A., Spiegel A.M., Boguski M.S., Roe B.A., Collins F.S.,
RA Burns A.L., Marx S.J., Chandrasekharappa S.C.;
RT "A transcript map for the 2.8-Mb region containing the multiple endocrine
RT neoplasia type 1 locus.";
RL Genome Res. 7:725-735(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10395801; DOI=10.1006/geno.1999.5800;
RA Mintz L., Galperin E., Pasmanik-Chor M., Tulzinsky S., Bromberg Y.,
RA Kozak C.A., Joyner A., Fein A., Horowitz M.;
RT "EHD1 -- an EH-domain-containing protein with a specific expression
RT pattern.";
RL Genomics 59:66-76(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Leukemia;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RT "Pediatric leukemia cDNA sequencing project.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-10.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH ZFYVE20, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15020713; DOI=10.1091/mbc.e03-10-0733;
RA Naslavsky N., Boehm M., Backlund P.S. Jr., Caplan S.;
RT "Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling
RT to the plasma membrane.";
RL Mol. Biol. Cell 15:2410-2422(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP INTERACTION WITH RAB11FIP2, SUBUNIT, ATP-BINDING SITE, AND MUTAGENESIS OF
RP GLY-65; VAL-203 AND TRP-485.
RX PubMed=16251358; DOI=10.1091/mbc.e05-05-0466;
RA Naslavsky N., Rahajeng J., Sharma M., Jovic M., Caplan S.;
RT "Interactions between EHD proteins and Rab11-FIP2: a role for EHD3 in early
RT endosomal transport.";
RL Mol. Biol. Cell 17:163-177(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17233914; DOI=10.1186/1471-2121-8-3;
RA George M., Ying G., Rainey M.A., Solomon A., Parikh P.T., Gao Q., Band V.,
RA Band H.;
RT "Shared as well as distinct roles of EHD proteins revealed by biochemical
RT and functional comparisons in mammalian cells and C. elegans.";
RL BMC Cell Biol. 8:3-3(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP INTERACTION WITH EHD4.
RX PubMed=18331452; DOI=10.1111/j.1600-0854.2008.00732.x;
RA Sharma M., Naslavsky N., Caplan S.;
RT "A role for EHD4 in the regulation of early endosomal transport.";
RL Traffic 9:995-1018(2008).
RN [13]
RP INTERACTION WITH MICALL1 AND RAB8A, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF LYS-483 AND TRP-485.
RX PubMed=19864458; DOI=10.1091/mbc.e09-06-0535;
RA Sharma M., Giridharan S.S., Rahajeng J., Naslavsky N., Caplan S.;
RT "MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor
RT recycling.";
RL Mol. Biol. Cell 20:5181-5194(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP FUNCTION IN ENDOCYTOSIS.
RX PubMed=20801876; DOI=10.1074/jbc.c110.166066;
RA Rahajeng J., Giridharan S.S., Naslavsky N., Caplan S.;
RT "Collapsin response mediator protein-2 (Crmp2) regulates trafficking by
RT linking endocytic regulatory proteins to dynein motors.";
RL J. Biol. Chem. 285:31918-31922(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP FUNCTION.
RX PubMed=24019528; DOI=10.1074/jbc.m113.488627;
RA Cai B., Giridharan S.S., Zhang J., Saxena S., Bahl K., Schmidt J.A.,
RA Sorgen P.L., Guo W., Naslavsky N., Caplan S.;
RT "Differential roles of C-terminal Eps15 homology domain proteins as
RT vesiculators and tubulators of recycling endosomes.";
RL J. Biol. Chem. 288:30172-30180(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-456, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP INTERACTION WITH PACSIN2, AND SUBCELLULAR LOCATION.
RX PubMed=23596323; DOI=10.1091/mbc.e13-01-0026;
RA Giridharan S.S., Cai B., Vitale N., Naslavsky N., Caplan S.;
RT "Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular
RT recycling endosome biogenesis.";
RL Mol. Biol. Cell 24:1776-1790(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-483 AND TRP-485.
RX PubMed=25686250; DOI=10.1038/ncb3109;
RA Lu Q., Insinna C., Ott C., Stauffer J., Pintado P.A., Rahajeng J., Baxa U.,
RA Walia V., Cuenca A., Hwang Y.S., Daar I.O., Lopes S.,
RA Lippincott-Schwartz J., Jackson P.K., Caplan S., Westlake C.J.;
RT "Early steps in primary cilium assembly require EHD1/EHD3-dependent ciliary
RT vesicle formation.";
RL Nat. Cell Biol. 17:228-240(2015).
RN [25]
RP ERRATUM OF PUBMED:25686250.
RA Lu Q., Insinna C., Ott C., Stauffer J., Pintado P.A., Rahajeng J., Baxa U.,
RA Walia V., Cuenca A., Hwang Y.S., Daar I.O., Lopes S.,
RA Lippincott-Schwartz J., Jackson P.K., Caplan S., Westlake C.J.;
RL Nat. Cell Biol. 17:531-531(2015).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [27]
RP STRUCTURE BY NMR OF 435-534 IN COMPLEX WITH MICALL1 PEPTIDE, AND
RP MUTAGENESIS OF LYS-468.
RX PubMed=20106972; DOI=10.1074/jbc.m109.045666;
RA Kieken F., Sharma M., Jovic M., Giridharan S.S., Naslavsky N., Caplan S.,
RA Sorgen P.L.;
RT "Mechanism for the selective interaction of C-terminal Eps15 homology
RT domain proteins with specific Asn-Pro-Phe-containing partners.";
RL J. Biol. Chem. 285:8687-8694(2010).
RN [28]
RP STRUCTURE BY NMR OF 401-534 IN COMPLEX WITH CALCIUM IONS.
RX PubMed=17899392; DOI=10.1007/s10858-007-9196-0;
RA Kieken F., Jovic M., Naslavsky N., Caplan S., Sorgen P.L.;
RT "EH domain of EHD1.";
RL J. Biomol. NMR 39:323-329(2007).
CC -!- FUNCTION: ATP- and membrane-binding protein that controls membrane
CC reorganization/tubulation upon ATP hydrolysis. In vitro causes
CC vesiculation of endocytic membranes (PubMed:24019528). Acts in early
CC endocytic membrane fusion and membrane trafficking of recycling
CC endosomes (PubMed:15020713, PubMed:17233914, PubMed:20801876).
CC Recruited to endosomal membranes upon nerve growth factor stimulation,
CC indirectly regulates neurite outgrowth (By similarity). Plays a role in
CC myoblast fusion (By similarity). Involved in the unidirectional
CC retrograde dendritic transport of endocytosed BACE1 and in efficient
CC sorting of BACE1 to axons implicating a function in neuronal APP
CC processing (By similarity). Plays a role in the formation of the
CC ciliary vesicle (CV), an early step in cilium biogenesis. Proposed to
CC be required for the fusion of distal appendage vesicles (DAVs) to form
CC the CV by recruiting SNARE complex component SNAP29. Is required for
CC recruitment of transition zone proteins CEP290, RPGRIP1L, TMEM67 and
CC B9D2, and of IFT20 following DAV reorganization before Rab8-dependent
CC ciliary membrane extension. Required for the loss of CCP110 form the
CC mother centriole essential for the maturation of the basal body during
CC ciliogenesis (PubMed:25686250). {ECO:0000250|UniProtKB:Q641Z6,
CC ECO:0000250|UniProtKB:Q9WVK4, ECO:0000269|PubMed:15020713,
CC ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:20801876,
CC ECO:0000269|PubMed:24019528, ECO:0000269|PubMed:25686250}.
CC -!- SUBUNIT: Homooligomer, and heterooligomer with EHD2, EHD3 and EHD4,
CC ATP-binding is required for heterooligomerization (PubMed:16251358,
CC PubMed:17233914, PubMed:18331452). Interacts (via EH domain) with
CC MICALL1 (via NPF1 motif); the interaction is direct and recruits EHD1
CC to membranes (PubMed:19864458, PubMed:20106972). Interacts with RAB35;
CC the interaction is indirect through MICALL1 and recruits EHD1 to
CC membranes (By similarity). Interacts (via EH domain) with PACSIN2 (via
CC NPF motifs); regulates localization to tubular recycling endosome
CC membranes (PubMed:23596323). Interacts with PACSIN1 (By similarity).
CC Interacts with RAB8A (PubMed:19864458). Interacts with FER1L5 (via
CC second C2 domain) (By similarity). Interacts with MYOF (By similarity).
CC Interacts with ZFYVE20 (PubMed:15020713). Interacts (via EH domain)
CC with RAB11FIP2 (PubMed:16251358). {ECO:0000250|UniProtKB:Q9WVK4,
CC ECO:0000269|PubMed:15020713, ECO:0000269|PubMed:16251358,
CC ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:17899392,
CC ECO:0000269|PubMed:18331452, ECO:0000269|PubMed:19864458,
CC ECO:0000269|PubMed:20106972, ECO:0000269|PubMed:23596323}.
CC -!- INTERACTION:
CC Q9H4M9; Q9P2R3: ANKFY1; NbExp=8; IntAct=EBI-490691, EBI-2513908;
CC Q9H4M9; Q9H4M9: EHD1; NbExp=4; IntAct=EBI-490691, EBI-490691;
CC Q9H4M9; Q9NZN3: EHD3; NbExp=8; IntAct=EBI-490691, EBI-2870749;
CC Q9H4M9; Q8N3F8: MICALL1; NbExp=12; IntAct=EBI-490691, EBI-1056885;
CC Q9H4M9; Q9H1K0: RBSN; NbExp=4; IntAct=EBI-490691, EBI-1105310;
CC Q9H4M9; O95721: SNAP29; NbExp=3; IntAct=EBI-490691, EBI-490676;
CC Q9H4M9; Q9QXY6: Ehd3; Xeno; NbExp=7; IntAct=EBI-490691, EBI-775304;
CC Q9H4M9; E1B9V6: RBSN; Xeno; NbExp=2; IntAct=EBI-490691, EBI-12509611;
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000269|PubMed:15020713, ECO:0000269|PubMed:17233914,
CC ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:23596323}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early
CC endosome membrane {ECO:0000269|PubMed:15020713}; Peripheral membrane
CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9WVK4}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, cilium
CC membrane {ECO:0000269|PubMed:25686250}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Preferentially
CC associates with tubular recycling endosomes (PubMed:15020713,
CC PubMed:17233914, PubMed:19864458, PubMed:23596323). Colocalizes with
CC FER1L5 at plasma membrane in myoblasts and myotubes (By similarity).
CC Localizes to the ciliary pocket from where the cilium protrudes
CC (PubMed:25686250). Colocalizes with BACE1 in tubulovesicular
CC cytoplasmic membranes. Colocalizes with BACE1 and APP amyloid beta
CC proteins in hippocampal mossy fiber terminals (By similarity).
CC {ECO:0000250|UniProtKB:Q9WVK4, ECO:0000269|PubMed:15020713,
CC ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:19864458,
CC ECO:0000269|PubMed:23596323, ECO:0000269|PubMed:25686250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:10395801}.
CC -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target
CC proteins. {ECO:0000250|UniProtKB:Q9WVK4}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. EHD subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01055}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF001434; AAB81204.1; -; mRNA.
DR EMBL; AF099011; AAD45866.1; -; mRNA.
DR EMBL; AY007161; AAG02009.1; -; mRNA.
DR EMBL; BC104799; AAI04800.1; -; mRNA.
DR EMBL; BC104825; AAI04826.1; -; mRNA.
DR CCDS; CCDS8084.1; -.
DR RefSeq; NP_001269373.1; NM_001282444.1.
DR RefSeq; NP_001269374.1; NM_001282445.1.
DR RefSeq; NP_006786.2; NM_006795.3.
DR RefSeq; XP_011543041.1; XM_011544739.1.
DR PDB; 2JQ6; NMR; -; A=401-534.
DR PDB; 2KFF; NMR; -; A=435-534.
DR PDB; 2KFG; NMR; -; A=435-534.
DR PDB; 2KFH; NMR; -; A=435-534.
DR PDB; 2KSP; NMR; -; A=435-534.
DR PDBsum; 2JQ6; -.
DR PDBsum; 2KFF; -.
DR PDBsum; 2KFG; -.
DR PDBsum; 2KFH; -.
DR PDBsum; 2KSP; -.
DR AlphaFoldDB; Q9H4M9; -.
DR BMRB; Q9H4M9; -.
DR SMR; Q9H4M9; -.
DR BioGRID; 116138; 159.
DR IntAct; Q9H4M9; 33.
DR MINT; Q9H4M9; -.
DR STRING; 9606.ENSP00000479153; -.
DR BindingDB; Q9H4M9; -.
DR ChEMBL; CHEMBL4295942; -.
DR iPTMnet; Q9H4M9; -.
DR MetOSite; Q9H4M9; -.
DR PhosphoSitePlus; Q9H4M9; -.
DR SwissPalm; Q9H4M9; -.
DR BioMuta; EHD1; -.
DR DMDM; 18202945; -.
DR CPTAC; CPTAC-68; -.
DR CPTAC; CPTAC-69; -.
DR EPD; Q9H4M9; -.
DR jPOST; Q9H4M9; -.
DR MassIVE; Q9H4M9; -.
DR MaxQB; Q9H4M9; -.
DR PaxDb; Q9H4M9; -.
DR PeptideAtlas; Q9H4M9; -.
DR PRIDE; Q9H4M9; -.
DR ProteomicsDB; 80867; -.
DR Antibodypedia; 44098; 179 antibodies from 29 providers.
DR DNASU; 10938; -.
DR Ensembl; ENST00000320631.8; ENSP00000320516.3; ENSG00000110047.18.
DR Ensembl; ENST00000359393.6; ENSP00000352354.2; ENSG00000110047.18.
DR GeneID; 10938; -.
DR KEGG; hsa:10938; -.
DR MANE-Select; ENST00000320631.8; ENSP00000320516.3; NM_006795.4; NP_006786.2.
DR UCSC; uc001obu.3; human.
DR CTD; 10938; -.
DR DisGeNET; 10938; -.
DR GeneCards; EHD1; -.
DR HGNC; HGNC:3242; EHD1.
DR HPA; ENSG00000110047; Tissue enhanced (bone marrow, testis).
DR MIM; 605888; gene.
DR neXtProt; NX_Q9H4M9; -.
DR OpenTargets; ENSG00000110047; -.
DR PharmGKB; PA27677; -.
DR VEuPathDB; HostDB:ENSG00000110047; -.
DR eggNOG; KOG1954; Eukaryota.
DR GeneTree; ENSGT00940000158249; -.
DR HOGENOM; CLU_017595_1_1_1; -.
DR InParanoid; Q9H4M9; -.
DR OMA; PFLKVHK; -.
DR OrthoDB; 933937at2759; -.
DR PhylomeDB; Q9H4M9; -.
DR TreeFam; TF314429; -.
DR PathwayCommons; Q9H4M9; -.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q9H4M9; -.
DR BioGRID-ORCS; 10938; 17 hits in 1081 CRISPR screens.
DR ChiTaRS; EHD1; human.
DR EvolutionaryTrace; Q9H4M9; -.
DR GeneWiki; EHD1; -.
DR GenomeRNAi; 10938; -.
DR Pharos; Q9H4M9; Tbio.
DR PRO; PR:Q9H4M9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9H4M9; protein.
DR Bgee; ENSG00000110047; Expressed in left testis and 198 other tissues.
DR ExpressionAtlas; Q9H4M9; baseline and differential.
DR Genevisible; Q9H4M9; HS.
DR GO; GO:0020018; C:ciliary pocket membrane; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; ISS:BHF-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0031095; C:platelet dense tubular network membrane; ISS:BHF-UCL.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; ISS:BHF-UCL.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; ISS:BHF-UCL.
DR GO; GO:2001137; P:positive regulation of endocytic recycling; ISS:UniProtKB.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IPI:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR CDD; cd00052; EH; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR040990; DUF5600.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR029951; EHD1/EHD3.
DR InterPro; IPR031692; EHD_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11216:SF127; PTHR11216:SF127; 1.
DR Pfam; PF18150; DUF5600; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF12763; EF-hand_4; 1.
DR Pfam; PF16880; EHD_N; 1.
DR SMART; SM00027; EH; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Calcium; Cell membrane;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Direct protein sequencing; Endosome; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..534
FT /note="EH domain-containing protein 1"
FT /id="PRO_0000146109"
FT DOMAIN 55..286
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 444..532
FT /note="EH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 476..511
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 65..72
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 91..92
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 153..156
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 219..222
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 243
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COILED 198..227
FT /evidence="ECO:0000255"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16251358"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT BINDING 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17899392, ECO:0007744|PDB:2KFG,
FT ECO:0007744|PDB:2KFH"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17899392, ECO:0007744|PDB:2KFG,
FT ECO:0007744|PDB:2KFH"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17899392, ECO:0007744|PDB:2KFG,
FT ECO:0007744|PDB:2KFH"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17899392, ECO:0007744|PDB:2KFG,
FT ECO:0007744|PDB:2KFH"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MUTAGEN 65
FT /note="G->R: Abolishes ATP-binding and localizes to
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:16251358"
FT MUTAGEN 203
FT /note="V->P: Greatly reduces oligomerization and
FT interaction with RAB11FIP2."
FT /evidence="ECO:0000269|PubMed:16251358"
FT MUTAGEN 468
FT /note="K->A: Loss of interaction with MICALL1."
FT /evidence="ECO:0000269|PubMed:20106972"
FT MUTAGEN 483
FT /note="K->E: Loss of accumulation at the ciliary pocket.
FT Loss of function in ciliogenesis. Loss of association with
FT tubulovesicular structures and altered MICALL1
FT localization. No effect on MICALL1 localization; when
FT associated with A-485."
FT /evidence="ECO:0000269|PubMed:19864458,
FT ECO:0000269|PubMed:25686250"
FT MUTAGEN 485
FT /note="W->A: Loss of accumulation at the ciliary pocket.
FT Loss of function in ciliogenesis. Abolishes interaction
FT with RAB11FIP2. No effect on MICALL1 localization; when
FT associated with E-483."
FT /evidence="ECO:0000269|PubMed:16251358,
FT ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:25686250"
FT CONFLICT 127
FT /note="A -> R (in Ref. 2; AAD45866)"
FT /evidence="ECO:0000305"
FT CONFLICT 180..182
FT /note="ERV -> DCW (in Ref. 2; AAD45866)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="L -> Q (in Ref. 2; AAD45866)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="D -> H (in Ref. 2; AAD45866)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="V -> M (in Ref. 2; AAD45866)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="D -> H (in Ref. 1; AAB81204)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="T -> S (in Ref. 2; AAD45866)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="A -> V (in Ref. 2; AAD45866)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="V -> E (in Ref. 2; AAD45866)"
FT /evidence="ECO:0000305"
FT CONFLICT 530..534
FT /note="KRRHE -> SAWGH (in Ref. 3; AAG02009)"
FT /evidence="ECO:0000305"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:2JQ6"
FT HELIX 445..454
FT /evidence="ECO:0007829|PDB:2JQ6"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:2JQ6"
FT HELIX 464..473
FT /evidence="ECO:0007829|PDB:2JQ6"
FT HELIX 478..488
FT /evidence="ECO:0007829|PDB:2JQ6"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:2JQ6"
FT HELIX 498..512
FT /evidence="ECO:0007829|PDB:2JQ6"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:2KFF"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:2JQ6"
SQ SEQUENCE 534 AA; 60627 MW; 3330218772A26CE4 CRC64;
MFSWVSKDAR RKKEPELFQT VAEGLRQLYA QKLLPLEEHY RFHEFHSPAL EDADFDNKPM
VLLVGQYSTG KTTFIRHLIE QDFPGMRIGP EPTTDSFIAV MHGPTEGVVP GNALVVDPRR
PFRKLNAFGN AFLNRFMCAQ LPNPVLDSIS IIDTPGILSG EKQRISRGYD FAAVLEWFAE
RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKIRVVLNK ADQIETQQLM RVYGALMWSL
GKIINTPEVV RVYIGSFWSH PLLIPDNRKL FEAEEQDLFK DIQSLPRNAA LRKLNDLIKR
ARLAKVHAYI ISSLKKEMPN VFGKESKKKE LVNNLGEIYQ KIEREHQISP GDFPSLRKMQ
ELLQTQDFSK FQALKPKLLD TVDDMLANDI ARLMVMVRQE ESLMPSQVVK GGAFDGTMNG
PFGHGYGEGA GEGIDDVEWV VGKDKPTYDE IFYTLSPVNG KITGANAKKE MVKSKLPNTV
LGKIWKLADV DKDGLLDDEE FALANHLIKV KLEGHELPAD LPPHLVPPSK RRHE
