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Q9NZN4 (EHD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
EH domain-containing protein 2
Alternative name(s):
PAST homolog 2
Gene names
Name:EHD2
Synonyms:PAST2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in membrane reorganization in response to nucleotide hydrolysis. Binds to liposomes and deforms them into tubules. Plays a role in membrane trafficking between the plasma membrane and endosomes. Important for the internalization of GLUT4. Required for normal fusion of myoblasts to skeletal muscle myotubes. Required for translocation of FER1L5 to the plasma membrane. Binds ATP; does not bind GTP By similarity. Ref.8

Enzyme regulation

The very low intrinsic ATPase activity is increased upon interaction with liposomes By similarity.

Subunit structure

Interacts with Asn-Pro-Phe (NPF) motifs in target proteins. Interacts with EHBP1. Interacts with FER1L5 (via second C2 domain) By similarity. Homodimer and homooligomer. Interacts with EHD1 and MYOF. May also interact with EHD3 and EHD4. Ref.8 Ref.9

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein By similarity. Note: Colocalizes with GLUT4 in intracellular tubulovesicular structures that are associated with cortical F-actin. Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes By similarity. Ref.8

Tissue specificity

Highly expressed in heart and moderately expressed in placenta, lung, and skeletal muscle.

Domain

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

Sequence similarities

Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. EHD subfamily.

Contains 1 dynamin-type G (guanine nucleotide-binding) domain.

Contains 1 EF-hand domain.

Contains 1 EH domain.

Ontologies

Keywords
   Cellular componentCell membrane
Endosome
Membrane
   Coding sequence diversityPolymorphism
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cortical actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

endocytic recycling

Inferred from genetic interaction Ref.8. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of endocytic recycling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of myoblast fusion

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentendosome membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleus

Traceable author statement Ref.1. Source: ProtInc

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

recycling endosome membrane

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP binding

Inferred from electronic annotation. Source: InterPro

GTPase activity

Inferred from electronic annotation. Source: InterPro

calcium ion binding

Inferred from electronic annotation. Source: InterPro

nucleic acid binding

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 543543EH domain-containing protein 2
PRO_0000146111

Regions

Domain55 – 286232Dynamin-type G
Domain449 – 53789EH
Domain481 – 51636EF-hand
Nucleotide binding65 – 728ATP By similarity
Calcium binding494 – 50512 By similarity

Sites

Binding site2201ATP By similarity
Binding site2581ATP By similarity

Amino acid modifications

Modified residue4381Phosphoserine Ref.7 Ref.10 Ref.11
Modified residue4681Phosphoserine Ref.10

Natural variations

Natural variant571G → S.
Corresponds to variant rs34140460 [ dbSNP | Ensembl ].
VAR_033917

Experimental info

Sequence conflict961C → F in AAF40470. Ref.1
Sequence conflict1641R → G in AAF40470. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9NZN4 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 0EBF691B0A707359

FASTA54361,161
        10         20         30         40         50         60 
MFSWLKRGGA RGQQPEAIRT VTSALKELYR TKLLPLEEHY RFGAFHSPAL EDADFDGKPM 

        70         80         90        100        110        120 
VLVAGQYSTG KTSFIQYLLE QEVPGSRVGP EPTTDCFVAV MHGDTEGTVP GNALVVDPDK 

       130        140        150        160        170        180 
PFRKLNPFGN TFLNRFMCAQ LPNQVLESIS IIDTPGILSG AKQRVSRGYD FPAVLRWFAE 

       190        200        210        220        230        240 
RVDLIILLFD AHKLEISDEF SEAIGALRGH EDKIRVVLNK ADMVETQQLM RVYGALMWAL 

       250        260        270        280        290        300 
GKVVGTPEVL RVYIGSFWSQ PLLVPDNRRL FELEEQDLFR DIQGLPRHAA LRKLNDLVKR 

       310        320        330        340        350        360 
ARLVRVHAYI ISYLKKEMPS VFGKENKKKQ LILKLPVIFA KIQLEHHISP GDFPDCQKMQ 

       370        380        390        400        410        420 
ELLMAHDFTK FHSLKPKLLE ALDEMLTHDI AKLMPLLRQE ELESTEVGVQ GGAFEGTHMG 

       430        440        450        460        470        480 
PFVERGPDEA MEDGEEGSDD EAEWVVTKDK SKYDEIFYNL APADGKLSGS KAKTWMVGTK 

       490        500        510        520        530        540 
LPNSVLGRIW KLSDVDRDGM LDDEEFALAS HLIEAKLEGH GLPANLPRRL VPPSKRRHKG 


SAE 

« Hide

References

« Hide 'large scale' references
[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].
Tissue: Fetal brain.
[2]"hEHD2, an EH domain containing protein-2."
Benjamin S., Horowitz M.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. expand/collapse author list , 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].
Tissue: Placenta.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Pancreas.
[6]"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-41; 168-176; 270-280 AND 342-358.
Tissue: Adipocyte.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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]"The endocytic recycling protein EHD2 interacts with myoferlin to regulate myoblast fusion."
Doherty K.R., Demonbreun A.R., Wallace G.Q., Cave A., Posey A.D., Heretis K., Pytel P., McNally E.M.
J. Biol. Chem. 283:20252-20260(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYOF.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438 AND SER-468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF181263 mRNA. Translation: AAF40470.1.
AF454952 mRNA. Translation: AAL51078.1.
AK315548 mRNA. Translation: BAG37926.1.
CH471126 Genomic DNA. Translation: EAW57505.1.
BC014445 mRNA. Translation: AAH14445.1.
CCDSCCDS12704.1.
RefSeqNP_055416.2. NM_014601.3.
UniGeneHs.744963.

3D structure databases

ProteinModelPortalQ9NZN4.
SMRQ9NZN4. Positions 1-539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119056. 15 interactions.
IntActQ9NZN4. 6 interactions.
STRING9606.ENSP00000263277.

PTM databases

PhosphoSiteQ9NZN4.

Polymorphism databases

DMDM57015322.

Proteomic databases

MaxQBQ9NZN4.
PaxDbQ9NZN4.
PeptideAtlasQ9NZN4.
PRIDEQ9NZN4.

Protocols and materials databases

DNASU30846.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263277; ENSP00000263277; ENSG00000024422.
GeneID30846.
KEGGhsa:30846.
UCSCuc002phj.4. human.

Organism-specific databases

CTD30846.
GeneCardsGC19P048216.
HGNCHGNC:3243. EHD2.
HPAHPA047394.
MIM605890. gene.
neXtProtNX_Q9NZN4.
PharmGKBPA27678.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0699.
HOGENOMHOG000242040.
HOVERGENHBG018183.
InParanoidQ9NZN4.
KOK12469.
OMAAPNEGKL.
OrthoDBEOG757CX9.
PhylomeDBQ9NZN4.
TreeFamTF314429.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ9NZN4.
BgeeQ9NZN4.
CleanExHS_EHD2.
GenevestigatorQ9NZN4.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR001401. 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]
PfamPF00350. Dynamin_N. 1 hit.
[Graphical view]
SMARTSM00027. EH. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50031. EH. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEHD2. human.
GeneWikiEHD2.
GenomeRNAi30846.
NextBio52972.
PROQ9NZN4.
SOURCESearch...

Entry information

Entry nameEHD2_HUMAN
AccessionPrimary (citable) accession number: Q9NZN4
Secondary accession number(s): B2RDH9, Q96CB6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 4, 2005
Last modified: July 9, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM