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Q9H4M9

- EHD1_HUMAN

UniProt

Q9H4M9 - EHD1_HUMAN

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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

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. 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
Complete GO annotation...

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: UniProtKB
  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
Complete GO annotation...

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

BgeeiQ9H4M9.
CleanExiHS_EHD1.
ExpressionAtlasiQ9H4M9. baseline and differential.
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. 47 interactions.
IntActiQ9H4M9. 5 interactions.
MINTiMINT-4999249.
STRINGi9606.ENSP00000320516.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JQ6NMR-A401-534[»]
2KFFNMR-A435-534[»]
2KFGNMR-A435-534[»]
2KFHNMR-A435-534[»]
2KSPNMR-A435-534[»]
ProteinModelPortaliQ9H4M9.
SMRiQ9H4M9. Positions 1-534.
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.
GeneTreeiENSGT00760000118985.
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

        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)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:
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_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:
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 .
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:
PDBei
RCSB PDBi
PDBji
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 1-534.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116138. 47 interactions.
IntActi Q9H4M9. 5 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.
GeneTreei ENSGT00760000118985.
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

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

Gene expression databases

Bgeei Q9H4M9.
CleanExi HS_EHD1.
ExpressionAtlasi Q9H4M9. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 127 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