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Protein

EH domain-containing protein 3

Gene

EHD3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis (PubMed:25686250). In vitro causes tubulation of endocytic membranes (PubMed:24019528). Binding to phosphatidic acid induces its membrane tubulation activity (By similarity). Plays a role in endocytic transport. Involved in early endosome to recycling endosome compartment (ERC), retrograde early endosome to Golgi, and endosome to plasma membrane (rapid recycling) protein transport. Involved in the regulation of Golgi maintenance and morphology (PubMed:16251358, PubMed:17233914, PubMed:19139087, PubMed:23781025). Involved in the recycling of internalized D1 dopamine receptor (PubMed:21791287). Plays a role in cardiac protein trafficking probably implicating ANK2 (PubMed:20489164). Involved in the ventricular membrane targeting of SLC8A1 and CACNA1C and probably the atrial membrane localization of CACNA1GG and CACNA1H implicated in the regulation of atrial myocyte exitability and cardiac conduction (By similarity). In conjunction with EHD4 may be involved in endocytic trafficking of KDR/VEGFR2 implicated in control of glomerular function (By similarity). Involved in the rapid recycling of integrin beta-3 implicated in cell adhesion maintenance (PubMed:23781025). Involved in the unidirectional retrograde dendritic transport of endocytosed BACE1 and in efficient sorting of BACE1 to axons implicating a function in neuronal APP processing (By similarity). Plays a role in the formation of the ciliary vesicle, an early step in cilium biogenesis; possibly sharing redundant functions with EHD1 (PubMed:25686250).By similarity1 Publication7 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 – 728ATP1 Publication
Calcium bindingi489 – 50012PROSITE-ProRule annotationBy similarityAdd
BLAST

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium ion binding Source: InterPro
  • GTP binding Source: InterPro
  • nucleic acid binding Source: ProtInc

GO - Biological processi

  • blood coagulation Source: Reactome
  • cilium assembly Source: UniProtKB
  • early endosome to Golgi transport Source: UniProtKB
  • endocytic recycling Source: UniProtKB
  • Golgi to lysosome transport Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein targeting to plasma membrane Source: MGI
  • receptor recycling Source: UniProtKB
  • regulation of cardiac muscle cell membrane potential Source: MGI
  • regulation of Golgi organization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Protein transport, Transport

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-HSA-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
EH domain-containing protein 3Curated
Alternative name(s):
PAST homolog 3Curated
Gene namesi
Name:EHD3Imported
Synonyms:EHD21 Publication, PAST3Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3244. EHD3.

Subcellular locationi

GO - Cellular componenti

  • ciliary pocket membrane Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: GOC
  • endocytic vesicle Source: Ensembl
  • endosome membrane Source: Reactome
  • focal adhesion Source: UniProtKB
  • myelin sheath Source: Ensembl
  • nucleus Source: ProtInc
  • perinuclear region of cytoplasm Source: Ensembl
  • recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, 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
Mutagenesisi315 – 3151K → R: Abolishes sumoylation and localization to tubular structures of the ERC, impairs fast recycling activity from the ERC, no effect on homooligomerization; when associated with R-511. 1 Publication
Mutagenesisi485 – 4851W → A: Abolishes interaction with RAB11FIP2. 1 Publication
Mutagenesisi511 – 5111K → R: Abolishes sumoylation localization to tubular structures of the ERC, impairs fast recycling activity from the ERC, no effect on homooligomerization;; when associated with R-315. 1 Publication

Organism-specific databases

PharmGKBiPA27679.

Polymorphism and mutation databases

BioMutaiEHD3.
DMDMi300669636.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 535535EH domain-containing protein 3PRO_0000146112Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Cross-linki315 – 315Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei349 – 3491PhosphoserineBy similarity
Modified residuei456 – 4561PhosphoserineBy similarity
Cross-linki511 – 511Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9NZN3.
MaxQBiQ9NZN3.
PaxDbiQ9NZN3.
PeptideAtlasiQ9NZN3.
PRIDEiQ9NZN3.

2D gel databases

OGPiQ9NZN3.

PTM databases

iPTMnetiQ9NZN3.
PhosphoSiteiQ9NZN3.

Expressioni

Tissue specificityi

Highly expressed in heart and brain and moderately expressed in kidney, liver, and placenta.1 Publication

Gene expression databases

BgeeiQ9NZN3.
CleanExiHS_EHD2.
HS_EHD3.
ExpressionAtlasiQ9NZN3. baseline and differential.
GenevisibleiQ9NZN3. HS.

Organism-specific databases

HPAiHPA049890.
HPA049986.

Interactioni

Subunit structurei

Homooligomer, and heterooligomer with EHD1, EHD2 and EHD4, ATP-binding is required for heterooligomerization (PubMed:16251358, PubMed:17233914). Interacts with PACSIN1 (By similarity). Interacts with PACSIN2 (By similarity). Interacts (via EH domain) with MICALL1 (PubMed:19864458). Interacts (via EH domain) with RAB11FIP2 (PubMed:16251358). Interacts with ANK2 (PubMed:20489164).By similarity5 Publications

Protein-protein interaction databases

BioGridi119055. 7 interactions.
IntActiQ9NZN3. 1 interaction.
STRINGi9606.ENSP00000327116.

Structurei

3D structure databases

ProteinModelPortaliQ9NZN3.
SMRiQ9NZN3. Positions 1-532.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG1954. Eukaryota.
ENOG410XYGB. LUCA.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000242040.
HOVERGENiHBG018183.
InParanoidiQ9NZN3.
KOiK12476.
OrthoDBiEOG757CX9.
PhylomeDBiQ9NZN3.
TreeFamiTF314429.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
3.40.50.300. 3 hits.
InterProiIPR022812. Dynamin_SF.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EH_dom.
IPR029951. EHD1/EHD3.
IPR031692. EHD_N.
IPR030381. G_DYNAMIN_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11216:SF67. PTHR11216:SF67. 1 hit.
PfamiPF00350. Dynamin_N. 1 hit.
PF12763. EF-hand_4. 1 hit.
PF16880. EHD_N. 1 hit.
[Graphical view]
SMARTiSM00027. EH. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF52540. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NZN3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFSWLGTDDR RRKDPEVFQT VSEGLKKLYK SKLLPLEEHY RFHEFHSPAL
60 70 80 90 100
EDADFDNKPM VLLVGQYSTG KTTFIRYLLE QDFPGMRIGP EPTTDSFIAV
110 120 130 140 150
MQGDMEGIIP GNALVVDPKK PFRKLNAFGN AFLNRFVCAQ LPNPVLESIS
160 170 180 190 200
VIDTPGILSG EKQRISRGYD FAAVLEWFAE RVDRIILLFD AHKLDISDEF
210 220 230 240 250
SEVIKALKNH EDKMRVVLNK ADQIETQQLM RVYGALMWSL GKIVNTPEVI
260 270 280 290 300
RVYIGSFWSH PLLIPDNRKL FEAEEQDLFR DIQSLPRNAA LRKLNDLIKR
310 320 330 340 350
ARLAKVHAYI ISSLKKEMPS VFGKDNKKKE LVNNLAEIYG RIEREHQISP
360 370 380 390 400
GDFPNLKRMQ DQLQAQDFSK FQPLKSKLLE VVDDMLAHDI AQLMVLVRQE
410 420 430 440 450
ESQRPIQMVK GGAFEGTLHG PFGHGYGEGA GEGIDDAEWV VARDKPMYDE
460 470 480 490 500
IFYTLSPVDG KITGANAKKE MVRSKLPNSV LGKIWKLADI DKDGMLDDDE
510 520 530
FALANHLIKV KLEGHELPNE LPAHLLPPSK RKVAE
Length:535
Mass (Da):60,887
Last modified:July 13, 2010 - v2
Checksum:i0F8AE99F84B966AD
GO
Isoform 2 (identifier: Q9NZN3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     169-175: YDFAAVL → PAAGPGL
     176-535: Missing.

Note: No experimental confirmation available.
Show »
Length:175
Mass (Da):19,584
Checksum:i6C1112ED8EEDEA46
GO

Sequence cautioni

The sequence AAF40471.1 differs from that shown. Reason: Frameshift at position 527. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei169 – 1757YDFAAVL → PAAGPGL in isoform 2. 1 PublicationVSP_056606
Alternative sequencei176 – 535360Missing in isoform 2. 1 PublicationVSP_056607Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF181264 mRNA. Translation: AAF40471.1. Frameshift.
AF214736 mRNA. Translation: AAF32285.1.
AK294222 mRNA. Translation: BAG57526.1.
AK316006 mRNA. Translation: BAH14377.1.
AL121657 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00480.1.
CH471053 Genomic DNA. Translation: EAX00481.1.
CCDSiCCDS1774.1. [Q9NZN3-1]
RefSeqiNP_055415.1. NM_014600.2. [Q9NZN3-1]
UniGeneiHs.368808.

Genome annotation databases

EnsembliENST00000322054; ENSP00000327116; ENSG00000013016. [Q9NZN3-1]
GeneIDi30845.
KEGGihsa:30845.
UCSCiuc002rnu.4. human. [Q9NZN3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF181264 mRNA. Translation: AAF40471.1. Frameshift.
AF214736 mRNA. Translation: AAF32285.1.
AK294222 mRNA. Translation: BAG57526.1.
AK316006 mRNA. Translation: BAH14377.1.
AL121657 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00480.1.
CH471053 Genomic DNA. Translation: EAX00481.1.
CCDSiCCDS1774.1. [Q9NZN3-1]
RefSeqiNP_055415.1. NM_014600.2. [Q9NZN3-1]
UniGeneiHs.368808.

3D structure databases

ProteinModelPortaliQ9NZN3.
SMRiQ9NZN3. Positions 1-532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119055. 7 interactions.
IntActiQ9NZN3. 1 interaction.
STRINGi9606.ENSP00000327116.

PTM databases

iPTMnetiQ9NZN3.
PhosphoSiteiQ9NZN3.

Polymorphism and mutation databases

BioMutaiEHD3.
DMDMi300669636.

2D gel databases

OGPiQ9NZN3.

Proteomic databases

EPDiQ9NZN3.
MaxQBiQ9NZN3.
PaxDbiQ9NZN3.
PeptideAtlasiQ9NZN3.
PRIDEiQ9NZN3.

Protocols and materials databases

DNASUi30845.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322054; ENSP00000327116; ENSG00000013016. [Q9NZN3-1]
GeneIDi30845.
KEGGihsa:30845.
UCSCiuc002rnu.4. human. [Q9NZN3-1]

Organism-specific databases

CTDi30845.
GeneCardsiEHD3.
H-InvDBHIX0001950.
HGNCiHGNC:3244. EHD3.
HPAiHPA049890.
HPA049986.
MIMi605891. gene.
neXtProtiNX_Q9NZN3.
PharmGKBiPA27679.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1954. Eukaryota.
ENOG410XYGB. LUCA.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000242040.
HOVERGENiHBG018183.
InParanoidiQ9NZN3.
KOiK12476.
OrthoDBiEOG757CX9.
PhylomeDBiQ9NZN3.
TreeFamiTF314429.

Enzyme and pathway databases

ReactomeiR-HSA-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiEHD3. human.
GenomeRNAii30845.
PROiQ9NZN3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NZN3.
CleanExiHS_EHD2.
HS_EHD3.
ExpressionAtlasiQ9NZN3. baseline and differential.
GenevisibleiQ9NZN3. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
3.40.50.300. 3 hits.
InterProiIPR022812. Dynamin_SF.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EH_dom.
IPR029951. EHD1/EHD3.
IPR031692. EHD_N.
IPR030381. G_DYNAMIN_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11216:SF67. PTHR11216:SF67. 1 hit.
PfamiPF00350. Dynamin_N. 1 hit.
PF12763. EF-hand_4. 1 hit.
PF16880. EHD_N. 1 hit.
[Graphical view]
SMARTiSM00027. EH. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF52540. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "EHD2, EHD3, and EHD4 encode novel members of a highly conserved family of EH domain-containing proteins."
    Pohl U., Smith J.S., Tachibana I., Ueki K., Lee H.K., Ramaswamy S., Wu Q., Mohrenweiser H.W., Jenkins R.B., Louis D.N.
    Genomics 63:255-262(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "EHD3: a protein that resides in recycling tubular and vesicular membrane structures and interacts with EHD1."
    Galperin E., Benjamin S., Rapaport D., Rotem-Yehudar R., Tolchinsky S., Horowitz M.
    Traffic 3:575-589(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Amygdala.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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, ACETYLATION AT MET-1.
    Tissue: Platelet.
  7. "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: FUNCTION, SUBUNIT, INTERACTION WITH RAB11FIP2, ATP-BINDING SITE, MUTAGENESIS OF GLY-65; VAL-203 AND TRP-485, SUBCELLULAR LOCATION.
  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. "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.
  10. "EHD3 regulates early-endosome-to-Golgi transport and preserves Golgi morphology."
    Naslavsky N., McKenzie J., Altan-Bonnet N., Sheff D., Caplan S.
    J. Cell Sci. 122:389-400(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "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.
  12. Cited for: FUNCTION, INTERACTION WITH ANK2, SUBCELLULAR LOCATION.
  13. "Endocytosis promotes rapid dopaminergic signaling."
    Kotowski S.J., Hopf F.W., Seif T., Bonci A., von Zastrow M.
    Neuron 71:278-290(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Differential roles of C-terminal Eps15 homology domain proteins as vesiculators and tubulators of recycling endosomes."
    Cai B., Giridharan S.S., Zhang J., Saxena S., Bahl K., Schmidt J.A., Sorgen P.L., Guo W., Naslavsky N., Caplan S.
    J. Biol. Chem. 288:30172-30180(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Alphavbeta3-integrin-mediated adhesion is regulated through an AAK1L- and EHD3-dependent rapid-recycling pathway."
    Waxmonsky N.C., Conner S.D.
    J. Cell Sci. 126:3593-3601(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  18. "SUMOylation of EHD3 Modulates Tubulation of the Endocytic Recycling Compartment."
    Cabasso O., Pekar O., Horowitz M.
    PLoS ONE 10:E0134053-E0134053(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, MUTAGENESIS OF LYS-315 AND LYS-511.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Chemical shift assignments of the C-terminal Eps15 homology domain-3 EH domain."
    Spagnol G., Reiling C., Kieken F., Caplan S., Sorgen P.L.
    Biomol. NMR. Assign. 8:263-267(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 433-535.

Entry informationi

Entry nameiEHD3_HUMAN
AccessioniPrimary (citable) accession number: Q9NZN3
Secondary accession number(s): B4DFR5
, D6W574, Q8N514, Q9NZB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: July 13, 2010
Last modified: July 6, 2016
This is version 130 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.