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Q9NZN3 (EHD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 3
Alternative name(s):
PAST homolog 3
Gene names
Name:EHD3
Synonyms:EHD2, PAST3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in endocytic transport. Ref.6

Subunit structure

Interacts with PACSIN1 By similarity. Homooligomer, and heterooligomer with EHD1, EHD2 and EHD4. Ref.6 Ref.7

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein. Cytoplasm By similarity Ref.6.

Tissue specificity

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

Domain

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

Sequence similarities

Contains 1 EF-hand domain.

Contains 1 EH domain.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 535535EH domain-containing protein 3
PRO_0000146112

Regions

Domain444 – 53289EH
Domain476 – 51136EF-hand
Nucleotide binding65 – 728ATP By similarity
Calcium binding489 – 50012 By similarity
Coiled coil198 – 22730 Potential

Sites

Binding site2201ATP By similarity
Binding site2581ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5
Modified residue4561Phosphoserine Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q9NZN3 [UniParc].

Last modified July 13, 2010. Version 2.
Checksum: 0F8AE99F84B966AD

FASTA53560,887
        10         20         30         40         50         60 
MFSWLGTDDR RRKDPEVFQT VSEGLKKLYK SKLLPLEEHY RFHEFHSPAL EDADFDNKPM 

        70         80         90        100        110        120 
VLLVGQYSTG KTTFIRYLLE QDFPGMRIGP EPTTDSFIAV MQGDMEGIIP GNALVVDPKK 

       130        140        150        160        170        180 
PFRKLNAFGN AFLNRFVCAQ LPNPVLESIS VIDTPGILSG EKQRISRGYD FAAVLEWFAE 

       190        200        210        220        230        240 
RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKMRVVLNK ADQIETQQLM RVYGALMWSL 

       250        260        270        280        290        300 
GKIVNTPEVI RVYIGSFWSH PLLIPDNRKL FEAEEQDLFR DIQSLPRNAA LRKLNDLIKR 

       310        320        330        340        350        360 
ARLAKVHAYI ISSLKKEMPS VFGKDNKKKE LVNNLAEIYG RIEREHQISP GDFPNLKRMQ 

       370        380        390        400        410        420 
DQLQAQDFSK FQPLKSKLLE VVDDMLAHDI AQLMVLVRQE ESQRPIQMVK GGAFEGTLHG 

       430        440        450        460        470        480 
PFGHGYGEGA GEGIDDAEWV VARDKPMYDE IFYTLSPVDG KITGANAKKE MVRSKLPNSV 

       490        500        510        520        530 
LGKIWKLADI DKDGMLDDDE FALANHLIKV KLEGHELPNE LPAHLLPPSK RKVAE 

« 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: 10673336] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"EHD2-EH domain containing 2, homolog of EHD1."
Galperin E., Benjamin S., Horowitz M.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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. expand/collapse author list , 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: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 12665801] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10, ACETYLATION AT MET-1.
Tissue: Platelet.
[6]"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: 17233914] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
[7]"A role for EHD4 in the regulation of early endosomal transport."
Sharma M., Naslavsky N., Caplan S.
Traffic 9:995-1018(2008) [PubMed: 18331452] [Abstract]
Cited for: INTERACTION WITH EHD4.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[9]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF181264 mRNA. Translation: AAF40471.1. Frameshift.
AF214736 mRNA. Translation: AAF32285.1.
AL121657 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00480.1.
CH471053 Genomic DNA. Translation: EAX00481.1.
IPIIPI00021458.
RefSeqNP_055415.1. NM_014600.2.
UniGeneHs.368808.

3D structure databases

ProteinModelPortalQ9NZN3.
SMRQ9NZN3. Positions 19-532.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9NZN3. 1 interaction.
STRINGQ9NZN3.

PTM databases

PhosphoSiteQ9NZN3.

Polymorphism databases

DMDM300669636.

2D gel databases

OGPQ9NZN3.

Proteomic databases

PRIDEQ9NZN3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322054; ENSP00000327116; ENSG00000013016.
GeneID30845.
KEGGhsa:30845.

Organism-specific databases

CTD30845.
GeneCardsGC02P031368.
H-InvDBHIX0001950.
HGNCHGNC:3244. EHD3.
MIM605891. gene.
neXtProtNX_Q9NZN3.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06454.
GeneTreeENSGT00600000084243.
HOGENOMHBG317590.
HOVERGENHBG018183.
InParanoidQ9NZN3.
OMAKVWKLAD.
OrthoDBEOG418BN4.
PhylomeDBQ9NZN3.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ9NZN3.
BgeeQ9NZN3.
CleanExHS_EHD2.
HS_EHD3.
GenevestigatorQ9NZN3.
GermOnlineENSG00000013016. Homo sapiens.

Family and domain databases

InterProIPR001401. Dynamin_GTPase.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR000261. EPS15_homology.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
KOK12476.
PfamPF00350. Dynamin_N. 1 hit.
[Graphical view]
SMARTSM00027. EH. 1 hit.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50031. EH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio52968.
SOURCESearch...

Entry information

Entry nameEHD3_HUMAN
AccessionPrimary (citable) accession number: Q9NZN3
Secondary accession number(s): D6W574, Q8N514, Q9NZB3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: July 13, 2010
Last modified: January 25, 2012
This is version 88 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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families