Q9NZN4 (EHD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
EH domain-containing protein 2

Alternative name(s):
PAST homolog 2

Gene names

Name:	EHD2
Synonyms:	PAST2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	543 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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 and MYOF 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 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	Contains 1 EF-hand domain. Contains 1 EH domain.

Ontologies

Keywords
Cellular component	Cell membrane Endosome Membrane
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC blood coagulation Traceable author statement. Source: Reactome cortical actin cytoskeleton organization Inferred from electronic annotation. Source: Compara endocytic recycling Inferred from genetic interaction Ref.8. Source: UniProtKB endocytosis Inferred from electronic annotation. Source: Compara
Cellular_component	nucleus Traceable author statement Ref.1. Source: ProtInc perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell recycling endosome membrane Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	ATP 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 543	543	EH domain-containing protein 2		PRO_0000146111
Regions
	Domain	449 – 537	89	EH
	Domain	481 – 516	36	EF-hand
	Nucleotide binding	65 – 72	8	ATP By similarity
	Calcium binding	494 – 505	12	By similarity
Sites
	Binding site	220	1	ATP By similarity
	Binding site	258	1	ATP By similarity
Amino acid modifications
	Modified residue	438	1	Phosphoserine Ref.7 Ref.10 Ref.11
	Modified residue	468	1	Phosphoserine Ref.10
Natural variations
	Natural variant	57	1	G → S. Corresponds to variant rs34140460 [ dbSNP | Ensembl ].		VAR_033917
Experimental info
	Sequence conflict	96	1	C → F in AAF40470. Ref.1
	Sequence conflict	164	1	R → G in AAF40470. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9NZN4 [UniParc]. Last modified January 4, 2005. Version 2. Checksum: 0EBF691B0A707359	FASTA	543	61,161
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
IPI	IPI00100980.
RefSeq	NP_055416.2. NM_014601.3.
UniGene	Hs.726547.
3D structure databases
ProteinModelPortal	Q9NZN4.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NZN4. 6 interactions.
STRING	9606.ENSP00000263277.
PTM databases
PhosphoSite	Q9NZN4.
Polymorphism databases
DMDM	57015322.
Proteomic databases
PaxDb	Q9NZN4.
PeptideAtlas	Q9NZN4.
PRIDE	Q9NZN4.
Protocols and materials databases
DNASU	30846.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263277; ENSP00000263277; ENSG00000024422.
GeneID	30846.
KEGG	hsa:30846.
UCSC	uc002phj.4. human.
Organism-specific databases
CTD	30846.
GeneCards	GC19P048216.
HGNC	HGNC:3243. EHD2.
MIM	605890. gene.
neXtProt	NX_Q9NZN4.
PharmGKB	PA27678.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0699.
HOGENOM	HOG000242040.
HOVERGEN	HBG018183.
InParanoid	Q9NZN4.
KO	K12469.
OMA	RKDNKKK.
OrthoDB	EOG4V437F.
PhylomeDB	Q9NZN4.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q9NZN4.
Bgee	Q9NZN4.
CleanEx	HS_EHD2.
Genevestigator	Q9NZN4.
GermOnline	ENSG00000024422. Homo sapiens.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR001401. Dynamin_GTPase. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR000261. EPS15_homology. [Graphical view]
Pfam	PF00350. Dynamin_N. 1 hit. [Graphical view]
SMART	SM00027. EH. 1 hit. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 1 hit. PS50031. EH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EHD2. human.
GenomeRNAi	30846.
NextBio	52972.
SOURCE	Search...

Entry information

Entry name

EHD2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.