Q9H4M9 (EHD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
EH domain-containing protein 1

Alternative name(s):
PAST homolog 1
Short name=hPAST1
Testilin

Gene names

Name:	EHD1
Synonyms:	PAST, PAST1
ORF Names:	CDABP0131

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	534 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Ref.6 Ref.8
Subunit structure	Interacts with PACSIN1 and PACSIN2 By similarity. Homooligomer, and heterooligomer with EHD2, EHD3 and EHD4. Interacts with ZFYVE20. Ref.6 Ref.8 Ref.11
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein. Note: Associated with intracellular tubulovesicular structures. Ref.6 Ref.8
Tissue specificity	Highly expressed in testis.
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
Domain	Coiled coil
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure 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 cholesterol homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL endocytic recycling Inferred from mutant phenotype Ref.6. Source: UniProtKB endocytosis Inferred from electronic annotation. Source: Compara intracellular protein transport Inferred from mutant phenotype Ref.6. Source: UniProtKB low-density lipoprotein particle clearance Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cholesterol storage Inferred from sequence or structural similarity. Source: BHF-UCL protein homooligomerization Inferred from physical interaction Ref.8. Source: UniProtKB
Cellular_component	early endosome membrane Inferred from direct assay Ref.6. Source: UniProtKB endocytic vesicle Inferred from electronic annotation. Source: Compara lipid particle Inferred from sequence or structural similarity. Source: BHF-UCL perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell platelet dense tubular network membrane Inferred from sequence or structural similarity. Source: BHF-UCL recycling endosome membrane Inferred from direct assay Ref.6Ref.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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 534

534

EH domain-containing protein 1

PRO_0000146109

Regions

Domain

444 – 532

89

EH

Domain

476 – 511

36

EF-hand

Nucleotide binding

65 – 72

8

ATP By similarity

Calcium binding

489 – 500

12

Coiled coil

198 – 227

30

Potential

Sites

Binding site

220

1

ATP By similarity

Binding site

258

1

ATP By similarity

Amino acid modifications

Modified residue

456

1

Phosphoserine Ref.10 Ref.12 Ref.13 Ref.15

Experimental info

Sequence conflict

127

1

A → R in AAD45866. Ref.2

Sequence conflict

180 – 182

3

ERV → DCW in AAD45866. Ref.2

Sequence conflict

194

1

L → Q in AAD45866. Ref.2

Sequence conflict

198

1

D → H in AAD45866. Ref.2

Sequence conflict

216

1

V → M in AAD45866. Ref.2

Sequence conflict

435

1

D → H in AAB81204. Ref.1

Sequence conflict

447

1

T → S in AAD45866. Ref.2

Sequence conflict

467

1

A → V in AAD45866. Ref.2

Sequence conflict

480

1

V → E in AAD45866. Ref.2

Sequence conflict

530 – 534

5

KRRHE → SAWGH in AAG02009. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

534

Helix Strand Turn

Details...

Helix

440 – 443

4

Helix

445 – 454

10

Beta strand

458 – 463

6

Helix

464 – 473

10

Helix

478 – 488

11

Beta strand

494 – 497

4

Helix

498 – 512

15

Turn

523 – 525

3

Helix

528 – 530

3

Sequences

	Sequence		Length	Mass (Da)
	Q9H4M9 [UniParc]. Last modified September 26, 2001. Version 2. Checksum: 3330218772A26CE4	FASTA	534	60,627
	10 20 30 40 50 60 MFSWVSKDAR RKKEPELFQT VAEGLRQLYA QKLLPLEEHY RFHEFHSPAL EDADFDNKPM 70 80 90 100 110 120 VLLVGQYSTG KTTFIRHLIE QDFPGMRIGP EPTTDSFIAV MHGPTEGVVP GNALVVDPRR 130 140 150 160 170 180 PFRKLNAFGN AFLNRFMCAQ LPNPVLDSIS IIDTPGILSG EKQRISRGYD FAAVLEWFAE 190 200 210 220 230 240 RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKIRVVLNK ADQIETQQLM RVYGALMWSL 250 260 270 280 290 300 GKIINTPEVV RVYIGSFWSH PLLIPDNRKL FEAEEQDLFK DIQSLPRNAA LRKLNDLIKR 310 320 330 340 350 360 ARLAKVHAYI ISSLKKEMPN VFGKESKKKE LVNNLGEIYQ KIEREHQISP GDFPSLRKMQ 370 380 390 400 410 420 ELLQTQDFSK FQALKPKLLD TVDDMLANDI ARLMVMVRQE ESLMPSQVVK GGAFDGTMNG 430 440 450 460 470 480 PFGHGYGEGA GEGIDDVEWV VGKDKPTYDE IFYTLSPVNG KITGANAKKE MVKSKLPNTV 490 500 510 520 530 LGKIWKLADV DKDGLLDDEE FALANHLIKV KLEGHELPAD LPPHLVPPSK RRHE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A transcript map for the 2.8-Mb region containing the multiple endocrine neoplasia type 1 locus." Guru S.C., Agarwal S.K., Manickam P., Olufemi S.-E., Crabtree J.S., Weisemann J.M., Kester M.B., Kim Y.S., Wang Y., Emmert-Buck M.R., Liotta L.A., Spiegel A.M., Boguski M.S., Roe B.A., Collins F.S., Burns A.L., Marx S.J., Chandrasekharappa S.C. Genome Res. 7:725-735(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"EHD1 -- an EH-domain-containing protein with a specific expression pattern." Mintz L., Galperin E., Pasmanik-Chor M., Tulzinsky S., Bromberg Y., Kozak C.A., Joyner A., Fein A., Horowitz M. Genomics 59:66-76(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Pediatric leukemia cDNA sequencing project." Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Leukemia.
[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.
[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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10. Tissue: Platelet.
[6]	"Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane." Naslavsky N., Boehm M., Backlund P.S. Jr., Caplan S. Mol. Biol. Cell 15:2410-2422(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH ZFYVE20, SUBCELLULAR LOCATION.
[7]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[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-456, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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-456, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, MASS SPECTROMETRY.
[16]	"EH domain of EHD1." Kieken F., Jovic M., Naslavsky N., Caplan S., Sorgen P.L. J. Biomol. NMR 39:323-329(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 401-534 IN COMPLEX WITH CALCIUM IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF001434 mRNA. Translation: AAB81204.1.
AF099011 mRNA. Translation: AAD45866.1.
AY007161 mRNA. Translation: AAG02009.1.
BC104799 mRNA. Translation: AAI04800.1.
BC104825 mRNA. Translation: AAI04826.1.

IPI

IPI00017184.

RefSeq

NP_006786.2. NM_006795.2.

UniGene

Hs.523774.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JQ6	NMR	-	A	401-534	[»]
2KFF	NMR	-	A	435-534	[»]
2KFG	NMR	-	A	435-534	[»]
2KFH	NMR	-	A	435-534	[»]
2KSP	NMR	-	A	435-534	[»]

ProteinModelPortal

Q9H4M9.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H4M9. 1 interaction.

MINT

MINT-4999249.

STRING

9606.ENSP00000320516.

PTM databases

PhosphoSite

Q9H4M9.

Polymorphism databases

DMDM

18202945.

Proteomic databases

PaxDb

Q9H4M9.

PeptideAtlas

Q9H4M9.

PRIDE

Q9H4M9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000320631; ENSP00000320516; ENSG00000110047.
ENST00000359393; ENSP00000352354; ENSG00000110047.

GeneID

10938.

KEGG

hsa:10938.

UCSC

uc001obu.1. human.

Organism-specific databases

CTD

10938.

GeneCards

GC11M064619.

H-InvDB

HIX0171322.

HGNC

HGNC:3242. EHD1.

MIM

605888. gene.

neXtProt

NX_Q9H4M9.

PharmGKB

PA27677.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG136252.

HOGENOM

HOG000242040.

HOVERGEN

HBG018183.

InParanoid

Q9H4M9.

KO

K12483.

OMA

QAYIISS.

OrthoDB

EOG418BN4.

PhylomeDB

Q9H4M9.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q9H4M9.

Bgee

Q9H4M9.

CleanEx

HS_EHD1.

Genevestigator

Q9H4M9.

GermOnline

ENSG00000110047. 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

EvolutionaryTrace

Q9H4M9.

GenomeRNAi

10938.

NextBio

41547.

SOURCE

Search...

Entry information

Entry name

EHD1_HUMAN

Accession

Primary (citable) accession number: Q9H4M9
Secondary accession number(s): O14611, Q2M3Q4, Q9UNR3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	September 26, 2001
Last modified:	May 1, 2013
This is version 109 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.