Q9H223 (EHD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
EH domain-containing protein 4

Alternative name(s):
Hepatocellular carcinoma-associated protein 10/11
PAST homolog 4

Gene names

Name:	EHD4
Synonyms:	HCA10, HCA11, PAST4
ORF Names:	FKSG7

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in early endosomal transport. Ref.8 Ref.10
Subunit structure	Homooligomer, and heterooligomer with EHD1, EHD2 and EHD3. Ref.8
Subcellular location	Cell membrane By similarity. Early endosome membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein Ref.10.
Tissue specificity	Highly expressed in pancreas and heart.
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
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to growth factor stimulus Inferred from electronic annotation. Source: Ensembl endocytic recycling Inferred from genetic interaction Ref.8. Source: UniProtKB pinocytosis Inferred from electronic annotation. Source: Ensembl positive regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Ensembl protein homooligomerization Inferred from physical interaction Ref.8. Source: UniProtKB regulation of endocytosis Inferred from electronic annotation. Source: Ensembl
Cellular_component	early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from direct assay. Source: LIFEdb extracellular vesicular exosome Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt nucleus Traceable author statement Ref.5. Source: ProtInc perinuclear region of cytoplasm Inferred from electronic annotation. Source: Ensembl 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.5. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 541	541	EH domain-containing protein 4		PRO_0000146114
Regions
	Domain	447 – 535	89	EH
	Domain	479 – 514	36	EF-hand
	Nucleotide binding	68 – 75	8	ATP By similarity
	Calcium binding	492 – 503	12	By similarity
Sites
	Binding site	223	1	ATP By similarity
	Binding site	261	1	ATP By similarity
Amino acid modifications
	Modified residue	451	1	Phosphotyrosine Ref.6
	Modified residue	459	1	Phosphoserine Ref.9 Ref.11
Natural variations
	Natural variant	154	1	V → I. Corresponds to variant rs11549015 [ dbSNP | Ensembl ].		VAR_053070
Experimental info
	Sequence conflict	297	1	L → I in AAG28784. Ref.2
	Sequence conflict	421 – 433	13	TEGPF…YGEGA → PRAPSTRATGRVP in AAG28784. Ref.2
	Sequence conflict	439	1	E → Q in AAG28784. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9H223 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 72DDE551829B7BF5	FASTA	541	61,175
	10 20 30 40 50 60 MFSWMGRQAG GRERAGGADA VQTVTGGLRS LYLRKVLPLE EAYRFHEFHS PALEDADFEN 70 80 90 100 110 120 KPMILLVGQY STGKTTFIRY LLEQDFPGMR IGPEPTTDSF IAVMYGETEG STPGNALVVD 130 140 150 160 170 180 PKKPFRKLSR FGNAFLNRFM CSQLPNQVLK SISVIDSPGI LSGEKQRISR GYDFCQVLQW 190 200 210 220 230 240 FAERVDRIIL LFDAHKLDIS DEFSEAIKAF RGQDDKIRVV LNKADQVDTQ QLMRVYGALM 250 260 270 280 290 300 WSLGKVINTP EVLRVYIGSF WAQPLQNTDN RRLFEAEAQD LFRDIQSLPQ KAAVRKLNDL 310 320 330 340 350 360 IKRARLAKVH AYIISYLKKE MPSVFGKENK KRELISRLPE IYIQLQREYQ ISAGDFPEVK 370 380 390 400 410 420 AMQEQLENYD FTKFHSLKPK LIEAVDNMLS NKISPLMNLI SQEETSTPTQ LVQGGAFDGT 430 440 450 460 470 480 TEGPFNQGYG EGAKEGADEE EWVVAKDKPV YDELFYTLSP INGKISGVNA KKEMVTSKLP 490 500 510 520 530 540 NSVLGKIWKL ADCDCDGMLD EEEFALAKHL IKIKLDGYEL PSSLPPHLVP PSHRKSLPKA D

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies." Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., Chen W.-F. J. Immunol. 169:1102-1109(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Hepatoma.
[2]	"Cloning of FKSG7, a novel gene which encodes an EH domain-containing protein." Wang Y.-G. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"hEHD4, an EH domain containing protein-4." Benjamin S., Horowitz M. Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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 and Placenta.
[5]	"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] OF 60-541. Tissue: Brain.
[6]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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: 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, SUBUNIT.
[9]	"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-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"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: FUNCTION, INTERACTION WITH EHD1 AND EHD3, SUBCELLULAR LOCATION.
[11]	"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-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF323924 mRNA. Translation: AAK11599.1. AF307137 mRNA. Translation: AAG28784.1. AF454953 mRNA. Translation: AAL51079.1. BC006287 mRNA. Translation: AAH06287.1. BC051823 mRNA. Translation: AAH51823.1. AF181265 mRNA. Translation: AAF40472.1.
RefSeq	NP_644670.1. NM_139265.3.
UniGene	Hs.143703.
3D structure databases
ProteinModelPortal	Q9H223.
SMR	Q9H223. Positions 22-535.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	119054. 21 interactions.
IntAct	Q9H223. 5 interactions.
MINT	MINT-5003543.
STRING	9606.ENSP00000220325.
PTM databases
PhosphoSite	Q9H223.
Polymorphism databases
DMDM	18202935.
Proteomic databases
PaxDb	Q9H223.
PeptideAtlas	Q9H223.
PRIDE	Q9H223.
Protocols and materials databases
DNASU	30844.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000220325; ENSP00000220325; ENSG00000103966.
GeneID	30844.
KEGG	hsa:30844.
UCSC	uc001zot.3. human.
Organism-specific databases
CTD	30844.
GeneCards	GC15M042190.
HGNC	HGNC:3245. EHD4.
HPA	HPA049890. HPA049986. HPA052729.
MIM	605892. gene.
neXtProt	NX_Q9H223.
PharmGKB	PA27680.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG136252.
HOGENOM	HOG000242040.
HOVERGEN	HBG018183.
InParanoid	Q9H223.
KO	K12477.
OMA	MPNQVLQ.
OrthoDB	EOG757CX9.
PhylomeDB	Q9H223.
TreeFam	TF314429.
Gene expression databases
Bgee	Q9H223.
CleanEx	HS_EHD4.
Genevestigator	Q9H223.
Family and domain databases
Gene3D	1.10.238.10. 1 hit. 3.40.50.300. 3 hits.
InterPro	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]
Pfam	PF00350. Dynamin_N. 1 hit. [Graphical view]
SMART	SM00027. EH. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 1 hit. PS50031. EH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GeneWiki	EHD4.
GenomeRNAi	30844.
NextBio	52964.
PRO	Q9H223.
SOURCE	Search...

Entry information

Entry name

EHD4_HUMAN

Accession

Primary (citable) accession number: Q9H223
Secondary accession number(s): Q9HAR1, Q9NZN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	March 1, 2001
Last modified:	April 16, 2014
This is version 124 of the entry and version 1 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.