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Protein

ADP-ribosylation factor 1

Gene

ARF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei160 – 1601GTP; via amide nitrogenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 329GTPCombined sourcesCurated
Nucleotide bindingi126 – 1294GTPCombined sourcesCurated

GO - Molecular functioni

  • GDP binding Source: Ensembl
  • GTPase activity Source: ProtInc
  • GTP binding Source: UniProtKB-KW
  • magnesium ion binding Source: Ensembl
  • phospholipase D activator activity Source: Ensembl
  • poly(A) RNA binding Source: UniProtKB
  • receptor signaling protein activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1660514. Synthesis of PIPs at the Golgi membrane.
R-HSA-167590. Nef Mediated CD4 Down-regulation.
R-HSA-199997. COPI Mediated Transport.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-421837. Clathrin derived vesicle budding.
R-HSA-432720. Lysosome Vesicle Biogenesis.
R-HSA-432722. Golgi Associated Vesicle Biogenesis.
R-HSA-6807878. COPI-mediated anterograde transport.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosylation factor 1
Gene namesi
Name:ARF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:652. ARF1.

Subcellular locationi

GO - Cellular componenti

  • cell leading edge Source: UniProtKB
  • COPI-coated vesicle Source: Ensembl
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi membrane Source: Reactome
  • late endosome Source: Ensembl
  • neuron projection Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • peroxisomal membrane Source: Ensembl
  • plasma membrane Source: ProtInc
  • postsynaptic density Source: UniProtKB-SubCell
  • postsynaptic membrane Source: UniProtKB-KW
  • sarcomere Source: Ensembl
  • trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24934.

Chemistry

ChEMBLiCHEMBL5985.

Polymorphism and mutation databases

BioMutaiARF1.
DMDMi51316985.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources2 Publications
Chaini2 – 181180ADP-ribosylation factor 1PRO_0000207378Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine; alternateCombined sources
Lipidationi2 – 21N-myristoyl glycine; alternate4 Publications

Post-translational modificationi

Demyristoylated by S.flexneri cysteine protease IpaJ which cleaves the peptide bond between N-myristoylated Gly-2 and Asn-3.2 Publications

Keywords - PTMi

Acetylation, Lipoprotein, Myristate

Proteomic databases

EPDiP84077.
MaxQBiP84077.
PaxDbiP84077.
PeptideAtlasiP84077.
PRIDEiP84077.
TopDownProteomicsiP84077.

PTM databases

iPTMnetiP84077.
PhosphoSiteiP84077.
SwissPalmiP84077.

Expressioni

Gene expression databases

BgeeiP84077.
CleanExiHS_ARF1.
ExpressionAtlasiP84077. baseline and differential.
GenevisibleiP84077. HS.

Organism-specific databases

HPAiCAB007742.

Interactioni

Subunit structurei

Interacts with ARHGAP21, ASAP2, GGA1, HERC1, PRKCABP, PIP5K1B, TMED2, PSCD2, TMED10 and GRIA2. Interacts with ARFGAP1, which hydrolyzes GTP and thus, regulates its function. Interacts with PI4KB in the Golgi complex. Interacts with NCS1/FREQ in the Golgi and at the plasma membrane. Interacts with PLEKHA3. Interacts with PLEKHA8; the interaction, together with phosphatidylinositol 4-phosphate binding, is required for FAPP2-mediated glucosylceramide transfer activity. Interacts (activated) with PICK1 (via PDZ domain); the interaction blocks Arp2/3 complex inhibition. Interacts with IQSEC1 (PubMed:24058294).9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CYTH2Q994184EBI-447171,EBI-448974
SPAG9O602713EBI-447171,EBI-1023301

Protein-protein interaction databases

BioGridi106870. 79 interactions.
DIPiDIP-31597N.
IntActiP84077. 27 interactions.
MINTiMINT-4999599.
STRINGi9606.ENSP00000272102.

Chemistry

BindingDBiP84077.

Structurei

Secondary structure

1
181
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 94Combined sources
Beta strandi10 – 123Combined sources
Beta strandi14 – 163Combined sources
Beta strandi19 – 257Combined sources
Helixi30 – 367Combined sources
Beta strandi42 – 454Combined sources
Beta strandi49 – 513Combined sources
Beta strandi53 – 586Combined sources
Beta strandi61 – 677Combined sources
Helixi72 – 787Combined sources
Helixi79 – 824Combined sources
Beta strandi85 – 939Combined sources
Beta strandi97 – 993Combined sources
Helixi100 – 11112Combined sources
Helixi114 – 1163Combined sources
Beta strandi120 – 1267Combined sources
Beta strandi131 – 1344Combined sources
Helixi136 – 1438Combined sources
Helixi145 – 1473Combined sources
Beta strandi153 – 1575Combined sources
Turni160 – 1634Combined sources
Helixi166 – 17914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HURX-ray2.00A/B2-181[»]
1RE0X-ray2.40A18-181[»]
1U81NMR-A18-181[»]
3O47X-ray2.80A/B11-181[»]
4HMYX-ray7.00C17-181[»]
ProteinModelPortaliP84077.
SMRiP84077. Positions 2-180.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP84077.

Family & Domainsi

Sequence similaritiesi

Belongs to the small GTPase superfamily. Arf family.Curated

Phylogenomic databases

eggNOGiKOG0070. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121855.
HOGENOMiHOG000163691.
HOVERGENiHBG002073.
InParanoidiP84077.
KOiK07937.
OMAiNDNERVS.
OrthoDBiEOG77WWDV.
PhylomeDBiP84077.
TreeFamiTF300808.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
PfamiPF00025. Arf. 1 hit.
[Graphical view]
PRINTSiPR00328. SAR1GTPBP.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51417. ARF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P84077-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG
60 70 80 90 100
FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV
110 120 130 140 150
NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH
160 170 180
RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ K
Length:181
Mass (Da):20,697
Last modified:January 23, 2007 - v2
Checksum:iAAC773D4A60186B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36340 mRNA. Translation: AAA35552.1.
M84326 mRNA. Translation: AAA35512.1.
AF052179 mRNA. Translation: AAC28623.1.
AF055002 mRNA. Translation: AAC09356.1.
AF493881 mRNA. Translation: AAM12595.1.
BT007393 mRNA. Translation: AAP36057.1.
AL136379 Genomic DNA. Translation: CAI23120.1.
BC009247 mRNA. Translation: AAH09247.1.
BC010429 mRNA. Translation: AAH10429.1.
BC011358 mRNA. Translation: AAH11358.1.
M84332 Genomic DNA. Translation: AAA35511.1.
CCDSiCCDS1565.1.
PIRiB40187. A33283.
RefSeqiNP_001019397.1. NM_001024226.1.
NP_001019398.1. NM_001024227.1.
NP_001019399.1. NM_001024228.1.
NP_001649.1. NM_001658.3.
UniGeneiHs.286221.

Genome annotation databases

EnsembliENST00000272102; ENSP00000272102; ENSG00000143761.
ENST00000540651; ENSP00000442980; ENSG00000143761.
ENST00000541182; ENSP00000440005; ENSG00000143761.
GeneIDi375.
KEGGihsa:375.
UCSCiuc001hrr.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36340 mRNA. Translation: AAA35552.1.
M84326 mRNA. Translation: AAA35512.1.
AF052179 mRNA. Translation: AAC28623.1.
AF055002 mRNA. Translation: AAC09356.1.
AF493881 mRNA. Translation: AAM12595.1.
BT007393 mRNA. Translation: AAP36057.1.
AL136379 Genomic DNA. Translation: CAI23120.1.
BC009247 mRNA. Translation: AAH09247.1.
BC010429 mRNA. Translation: AAH10429.1.
BC011358 mRNA. Translation: AAH11358.1.
M84332 Genomic DNA. Translation: AAA35511.1.
CCDSiCCDS1565.1.
PIRiB40187. A33283.
RefSeqiNP_001019397.1. NM_001024226.1.
NP_001019398.1. NM_001024227.1.
NP_001019399.1. NM_001024228.1.
NP_001649.1. NM_001658.3.
UniGeneiHs.286221.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HURX-ray2.00A/B2-181[»]
1RE0X-ray2.40A18-181[»]
1U81NMR-A18-181[»]
3O47X-ray2.80A/B11-181[»]
4HMYX-ray7.00C17-181[»]
ProteinModelPortaliP84077.
SMRiP84077. Positions 2-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106870. 79 interactions.
DIPiDIP-31597N.
IntActiP84077. 27 interactions.
MINTiMINT-4999599.
STRINGi9606.ENSP00000272102.

Chemistry

BindingDBiP84077.
ChEMBLiCHEMBL5985.

PTM databases

iPTMnetiP84077.
PhosphoSiteiP84077.
SwissPalmiP84077.

Polymorphism and mutation databases

BioMutaiARF1.
DMDMi51316985.

Proteomic databases

EPDiP84077.
MaxQBiP84077.
PaxDbiP84077.
PeptideAtlasiP84077.
PRIDEiP84077.
TopDownProteomicsiP84077.

Protocols and materials databases

DNASUi375.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272102; ENSP00000272102; ENSG00000143761.
ENST00000540651; ENSP00000442980; ENSG00000143761.
ENST00000541182; ENSP00000440005; ENSG00000143761.
GeneIDi375.
KEGGihsa:375.
UCSCiuc001hrr.4. human.

Organism-specific databases

CTDi375.
GeneCardsiARF1.
H-InvDBHIX0116279.
HGNCiHGNC:652. ARF1.
HPAiCAB007742.
MIMi103180. gene.
neXtProtiNX_P84077.
PharmGKBiPA24934.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0070. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121855.
HOGENOMiHOG000163691.
HOVERGENiHBG002073.
InParanoidiP84077.
KOiK07937.
OMAiNDNERVS.
OrthoDBiEOG77WWDV.
PhylomeDBiP84077.
TreeFamiTF300808.

Enzyme and pathway databases

ReactomeiR-HSA-1660514. Synthesis of PIPs at the Golgi membrane.
R-HSA-167590. Nef Mediated CD4 Down-regulation.
R-HSA-199997. COPI Mediated Transport.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-421837. Clathrin derived vesicle budding.
R-HSA-432720. Lysosome Vesicle Biogenesis.
R-HSA-432722. Golgi Associated Vesicle Biogenesis.
R-HSA-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

ChiTaRSiARF1. human.
EvolutionaryTraceiP84077.
GeneWikiiARF1.
GenomeRNAii375.
NextBioi1569.
PROiP84077.
SOURCEiSearch...

Gene expression databases

BgeeiP84077.
CleanExiHS_ARF1.
ExpressionAtlasiP84077. baseline and differential.
GenevisibleiP84077. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
PfamiPF00025. Arf. 1 hit.
[Graphical view]
PRINTSiPR00328. SAR1GTPBP.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51417. ARF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, characterization, and expression of human ADP-ribosylation factors: two guanine nucleotide-dependent activators of cholera toxin."
    Bobak D.A., Nightingale M.S., Murtagh J.J. Jr., Price S.R., Moss J., Vaughan M.
    Proc. Natl. Acad. Sci. U.S.A. 86:6101-6105(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins."
    Kahn R.A., Kern F.G., Clark J., Gelmann E.P., Rulka C.
    J. Biol. Chem. 266:2606-2614(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin."
    Lee C.M., Haun R.S., Tsai S.C., Moss J., Vaughan M.
    J. Biol. Chem. 267:9028-9034(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Large-scale concatenation cDNA sequencing."
    Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
    Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Cervix, Eye and Kidney.
  9. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 20-30; 80-97 AND 118-142, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  10. "p619, a giant protein related to the chromosome condensation regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab proteins."
    Rosa J.L., Casaroli-Marano R.P., Buckler A.J., Vilaro S., Barbacid M.
    EMBO J. 15:4262-4273(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HERC1.
  11. "Identification of a new Pyk2 target protein with Arf-GAP activity."
    Andreev J., Simon J.-P., Sabatini D.D., Kam J., Plowman G., Randazzo P.A., Schlessinger J.
    Mol. Cell. Biol. 19:2338-2350(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ASAP2.
  12. "FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P."
    Godi A., Di Campli A., Konstantakopoulos A., Di Tullio G., Alessi D.R., Kular G.S., Daniele T., Marra P., Lucocq J.M., De Matteis M.A.
    Nat. Cell Biol. 6:393-404(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLEKHA8.
  13. "Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi membranes."
    Menetrey J., Perderiset M., Cicolari J., Dubois T., Elkhatib N., El Khadali F., Franco M., Chavrier P., Houdusse A.
    EMBO J. 26:1953-1962(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGAP21.
  14. "Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta."
    Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.
    Traffic 8:1080-1092(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PI4KB AND NCS1, SUBCELLULAR LOCATION.
  15. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
    Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
    Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain."
    He J., Scott J.L., Heroux A., Roy S., Lenoir M., Overduin M., Stahelin R.V., Kutateladze T.G.
    J. Biol. Chem. 286:18650-18657(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLEKHA3.
  19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Proteolytic elimination of N-myristoyl modifications by the Shigella virulence factor IpaJ."
    Burnaevskiy N., Fox T.G., Plymire D.A., Ertelt J.M., Weigele B.A., Selyunin A.S., Way S.S., Patrie S.M., Alto N.M.
    Nature 496:106-109(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, DEMYRISTOYLATION.
  21. "The small GTPase Arf1 modulates Arp2/3-mediated actin polymerization via PICK1 to regulate synaptic plasticity."
    Rocca D.L., Amici M., Antoniou A., Suarez E.B., Halemani N., Murk K., McGarvey J., Jaafari N., Mellor J.R., Collingridge G.L., Hanley J.G.
    Neuron 79:293-307(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PICK1 AND GRIA2.
  22. "Integrated conformational and lipid-sensing regulation of endosomal ArfGEF BRAG2."
    Aizel K., Biou V., Navaza J., Duarte L.V., Campanacci V., Cherfils J., Zeghouf M.
    PLoS Biol. 11:E1001652-E1001652(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IQSEC1.
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "Global profiling of co- and post-translationally N-myristoylated proteomes in human cells."
    Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.
    Nat. Commun. 5:4919-4919(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
  25. "Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development."
    Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I., Tate E.W.
    Angew. Chem. Int. Ed. 54:5948-5951(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Structure of the human ADP-ribosylation factor 1 complexed with GDP."
    Amor J.C., Harrison D.H., Kahn R.A., Ringe D.
    Nature 372:704-708(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH GDP.
  28. "Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis."
    Goldberg J.
    Cell 96:893-902(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RAT ARFGAP1 CATALYTIC DOMAIN.
  29. "Crystal structure of ARF1*Sec7 complexed with brefeldin A and its implications for the guanine nucleotide exchange mechanism."
    Mossessova E., Corpina R.A., Goldberg J.
    Mol. Cell 12:1403-1411(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-181 IN COMPLEX WITH GDP; BREFELDIN AND YEAST GEA1.
  30. "Conformational changes in human Arf1 on nucleotide exchange and deletion of membrane-binding elements."
    Seidel R.D., Amor J.C., Kahn R.A., Prestegard J.H.
    J. Biol. Chem. 279:48307-48318(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 18-181 IN COMPLEX WITH GDP.
  31. "Crystal structure of ARFGAP1-ARF1 fusion protein."
    Structural genomics consortium (SGC).
    Submitted (JUL-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 11-181 IN COMPLEX WITH GDP.

Entry informationi

Entry nameiARF1_HUMAN
AccessioniPrimary (citable) accession number: P84077
Secondary accession number(s): P10947, P32889
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.