Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9H4M9

- EHD1_HUMAN

UniProt

Q9H4M9 - EHD1_HUMAN

Protein

EH domain-containing protein 1

Gene

EHD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei220 – 2201ATPBy similarity
    Binding sitei258 – 2581ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi65 – 728ATP
    Calcium bindingi489 – 50012Add
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium ion binding Source: InterPro
    3. GTPase activity Source: InterPro
    4. GTP binding Source: InterPro
    5. protein binding Source: UniProtKB
    6. Rab GTPase binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cellular response to nerve growth factor stimulus Source: UniProtKB
    3. cholesterol homeostasis Source: BHF-UCL
    4. endocytic recycling Source: UniProtKB
    5. endocytosis Source: UniProtKB
    6. intracellular protein transport Source: UniProtKB
    7. low-density lipoprotein particle clearance Source: BHF-UCL
    8. neuron projection development Source: UniProtKB
    9. positive regulation of cholesterol storage Source: BHF-UCL
    10. positive regulation of endocytic recycling Source: UniProtKB
    11. positive regulation of myoblast fusion Source: UniProtKB
    12. protein homooligomerization Source: UniProtKB

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    EH domain-containing protein 1
    Alternative name(s):
    PAST homolog 1
    Short name:
    hPAST1
    Testilin
    Gene namesi
    Name:EHD1
    Synonyms:PAST, PAST1
    ORF Names:CDABP0131
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3242. EHD1.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. early endosome membrane Source: UniProtKB
    2. endocytic vesicle Source: Ensembl
    3. endosome membrane Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. lipid particle Source: BHF-UCL
    6. membrane Source: UniProtKB
    7. perinuclear region of cytoplasm Source: Ensembl
    8. plasma membrane Source: UniProtKB
    9. platelet dense tubular network membrane Source: BHF-UCL
    10. recycling endosome membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi65 – 651G → R: Abolishes ATP-binding and localizes to cytoplasm. 1 Publication
    Mutagenesisi203 – 2031V → P: Greatly reduces oligomerization and interaction with RAB11FIP2. 1 Publication
    Mutagenesisi468 – 4681K → A: Loss of interaction with MICALL1. 1 Publication
    Mutagenesisi483 – 4831K → E: Loss of association with tubulovesicular structures and altered MICALL1 localization. No effect on MICALL1 localization; when associated with A-485. 1 Publication
    Mutagenesisi485 – 4851W → A: Abolishes interaction with RAB11FIP2. 2 Publications
    Mutagenesisi485 – 4851W → A: No effect on MICALL1 localization; when associated with E-483. 2 Publications

    Organism-specific databases

    PharmGKBiPA27677.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 534534EH domain-containing protein 1PRO_0000146109Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei456 – 4561Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H4M9.
    PaxDbiQ9H4M9.
    PeptideAtlasiQ9H4M9.
    PRIDEiQ9H4M9.

    PTM databases

    PhosphoSiteiQ9H4M9.

    Expressioni

    Tissue specificityi

    Highly expressed in testis.

    Gene expression databases

    ArrayExpressiQ9H4M9.
    BgeeiQ9H4M9.
    CleanExiHS_EHD1.
    GenevestigatoriQ9H4M9.

    Interactioni

    Subunit structurei

    Homooligomer, and heterooligomer with EHD2, EHD3 and EHD4, ATP-binding is required for heterooligomerization. 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. Interacts (via EH domain) with RAB11FIP2.8 Publications

    Protein-protein interaction databases

    BioGridi116138. 41 interactions.
    IntActiQ9H4M9. 4 interactions.
    MINTiMINT-4999249.
    STRINGi9606.ENSP00000320516.

    Structurei

    Secondary structure

    1
    534
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi440 – 4434
    Helixi445 – 45410
    Beta strandi458 – 4636
    Helixi464 – 47310
    Helixi478 – 48811
    Beta strandi494 – 4974
    Helixi498 – 51215
    Turni523 – 5253
    Helixi528 – 5303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JQ6NMR-A401-534[»]
    2KFFNMR-A435-534[»]
    2KFGNMR-A435-534[»]
    2KFHNMR-A435-534[»]
    2KSPNMR-A435-534[»]
    ProteinModelPortaliQ9H4M9.
    SMRiQ9H4M9. Positions 19-534.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H4M9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 286232Dynamin-type GAdd
    BLAST
    Domaini444 – 53289EHPROSITE-ProRule annotationAdd
    BLAST
    Domaini476 – 51136EF-handPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili198 – 22730Sequence AnalysisAdd
    BLAST

    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

    eggNOGiNOG136252.
    HOGENOMiHOG000242040.
    HOVERGENiHBG018183.
    InParanoidiQ9H4M9.
    KOiK12483.
    OMAiQAYIISS.
    OrthoDBiEOG757CX9.
    PhylomeDBiQ9H4M9.
    TreeFamiTF314429.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR001401. 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]
    PfamiPF00350. Dynamin_N. 1 hit.
    [Graphical view]
    SMARTiSM00027. EH. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. 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

    MFSWVSKDAR RKKEPELFQT VAEGLRQLYA QKLLPLEEHY RFHEFHSPAL    50
    EDADFDNKPM VLLVGQYSTG KTTFIRHLIE QDFPGMRIGP EPTTDSFIAV 100
    MHGPTEGVVP GNALVVDPRR PFRKLNAFGN AFLNRFMCAQ LPNPVLDSIS 150
    IIDTPGILSG EKQRISRGYD FAAVLEWFAE RVDRIILLFD AHKLDISDEF 200
    SEVIKALKNH EDKIRVVLNK ADQIETQQLM RVYGALMWSL GKIINTPEVV 250
    RVYIGSFWSH PLLIPDNRKL FEAEEQDLFK DIQSLPRNAA LRKLNDLIKR 300
    ARLAKVHAYI ISSLKKEMPN VFGKESKKKE LVNNLGEIYQ KIEREHQISP 350
    GDFPSLRKMQ ELLQTQDFSK FQALKPKLLD TVDDMLANDI ARLMVMVRQE 400
    ESLMPSQVVK GGAFDGTMNG PFGHGYGEGA GEGIDDVEWV VGKDKPTYDE 450
    IFYTLSPVNG KITGANAKKE MVKSKLPNTV LGKIWKLADV DKDGLLDDEE 500
    FALANHLIKV KLEGHELPAD LPPHLVPPSK RRHE 534
    Length:534
    Mass (Da):60,627
    Last modified:September 26, 2001 - v2
    Checksum:i3330218772A26CE4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti127 – 1271A → R in AAD45866. (PubMed:10395801)Curated
    Sequence conflicti180 – 1823ERV → DCW in AAD45866. (PubMed:10395801)Curated
    Sequence conflicti194 – 1941L → Q in AAD45866. (PubMed:10395801)Curated
    Sequence conflicti198 – 1981D → H in AAD45866. (PubMed:10395801)Curated
    Sequence conflicti216 – 2161V → M in AAD45866. (PubMed:10395801)Curated
    Sequence conflicti435 – 4351D → H in AAB81204. (PubMed:9253601)Curated
    Sequence conflicti447 – 4471T → S in AAD45866. (PubMed:10395801)Curated
    Sequence conflicti467 – 4671A → V in AAD45866. (PubMed:10395801)Curated
    Sequence conflicti480 – 4801V → E in AAD45866. (PubMed:10395801)Curated
    Sequence conflicti530 – 5345KRRHE → SAWGH in AAG02009. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_006718487.1. XM_006718424.1.
    UniGeneiHs.523774.
    Hs.708818.

    Genome annotation databases

    EnsembliENST00000320631; ENSP00000320516; ENSG00000110047.
    ENST00000359393; ENSP00000352354; ENSG00000110047.
    GeneIDi10938.
    KEGGihsa:10938.
    UCSCiuc001obu.1. human.

    Polymorphism databases

    DMDMi18202945.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS8084.1.
    RefSeqi NP_001269373.1. NM_001282444.1.
    NP_001269374.1. NM_001282445.1.
    NP_006786.2. NM_006795.3.
    XP_006718487.1. XM_006718424.1.
    UniGenei Hs.523774.
    Hs.708818.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JQ6 NMR - A 401-534 [» ]
    2KFF NMR - A 435-534 [» ]
    2KFG NMR - A 435-534 [» ]
    2KFH NMR - A 435-534 [» ]
    2KSP NMR - A 435-534 [» ]
    ProteinModelPortali Q9H4M9.
    SMRi Q9H4M9. Positions 19-534.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116138. 41 interactions.
    IntActi Q9H4M9. 4 interactions.
    MINTi MINT-4999249.
    STRINGi 9606.ENSP00000320516.

    PTM databases

    PhosphoSitei Q9H4M9.

    Polymorphism databases

    DMDMi 18202945.

    Proteomic databases

    MaxQBi Q9H4M9.
    PaxDbi Q9H4M9.
    PeptideAtlasi Q9H4M9.
    PRIDEi Q9H4M9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000320631 ; ENSP00000320516 ; ENSG00000110047 .
    ENST00000359393 ; ENSP00000352354 ; ENSG00000110047 .
    GeneIDi 10938.
    KEGGi hsa:10938.
    UCSCi uc001obu.1. human.

    Organism-specific databases

    CTDi 10938.
    GeneCardsi GC11M064619.
    H-InvDB HIX0171322.
    HGNCi HGNC:3242. EHD1.
    MIMi 605888. gene.
    neXtProti NX_Q9H4M9.
    PharmGKBi PA27677.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG136252.
    HOGENOMi HOG000242040.
    HOVERGENi HBG018183.
    InParanoidi Q9H4M9.
    KOi K12483.
    OMAi QAYIISS.
    OrthoDBi EOG757CX9.
    PhylomeDBi Q9H4M9.
    TreeFami TF314429.

    Enzyme and pathway databases

    Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    EvolutionaryTracei Q9H4M9.
    GeneWikii EHD1.
    GenomeRNAii 10938.
    NextBioi 41547.
    PROi Q9H4M9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H4M9.
    Bgeei Q9H4M9.
    CleanExi HS_EHD1.
    Genevestigatori Q9H4M9.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR001401. 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 ]
    Pfami PF00350. Dynamin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00027. EH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS50031. EH. 1 hit.
    PS51718. G_DYNAMIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "Interactions between EHD proteins and Rab11-FIP2: a role for EHD3 in early endosomal transport."
      Naslavsky N., Rahajeng J., Sharma M., Jovic M., Caplan S.
      Mol. Biol. Cell 17:163-177(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB11FIP2, SUBUNIT, ATP-BINDING SITE, MUTAGENESIS OF GLY-65; VAL-203 AND TRP-485, SUBCELLULAR LOCATION.
    9. "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.
    10. "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.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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.
    13. "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.
    14. "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.
    15. "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.
    16. "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.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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].
    19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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.
    21. "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.
    22. Cited for: STRUCTURE BY NMR OF 401-534 IN COMPLEX WITH CALCIUM IONS.

    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: October 1, 2014
    This is version 125 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

    External Data

    Dasty 3