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Q9H4M9

- EHD1_HUMAN

UniProt

Q9H4M9 - EHD1_HUMAN

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Protein
EH domain-containing protein 1
Gene
EHD1, PAST, PAST1, CDABP0131
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 – 2201ATP By similarity
Binding sitei258 – 2581ATP By similarity

Regions

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

GO - Molecular functioni

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

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. perinuclear region of cytoplasm Source: Ensembl
  7. plasma membrane Source: UniProtKB
  8. platelet dense tubular network membrane Source: BHF-UCL
  9. recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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: No effect on MICALL1 localization; when associated with E-483. 1 Publication

Organism-specific databases

PharmGKBiPA27677.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 534534EH domain-containing protein 1
PRO_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. 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 ZFYVE20.5 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ9H4M9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 286232Dynamin-type G
Add
BLAST
Domaini444 – 53289EH
Add
BLAST
Domaini476 – 51136EF-hand
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili198 – 22730 Reviewed prediction
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 EF-hand domain.
Contains 1 EH domain.

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

Sequence conflict

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

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

« 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. "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. 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. 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. 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. 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: September 3, 2014
This is version 124 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

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