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ADP-ribosylation factor 1

 ARF1_HUMAN              Reviewed;         181 AA.
P84077; P10947; P32889;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-DEC-2018, entry version 169.
RecName: Full=ADP-ribosylation factor 1;
Name=ARF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2474826; DOI=10.1073/pnas.86.16.6101;
Bobak D.A., Nightingale M.S., Murtagh J.J. Jr., Price S.R., Moss J.,
Vaughan M.;
"Molecular cloning, characterization, and expression of human ADP-
ribosylation factors: two guanine nucleotide-dependent activators of
cholera toxin.";
Proc. Natl. Acad. Sci. U.S.A. 86:6101-6105(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1899243;
Kahn R.A., Kern F.G., Clark J., Gelmann E.P., Rulka C.;
"Human ADP-ribosylation factors. A functionally conserved family of
GTP-binding proteins.";
J. Biol. Chem. 266:2606-2614(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1577740;
Lee C.M., Haun R.S., Tsai S.C., Moss J., Vaughan M.;
"Characterization of the human gene encoding ADP-ribosylation factor
1, a guanine nucleotide-binding activator of cholera toxin.";
J. Biol. Chem. 267:9028-9034(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=9110174;
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.;
"Large-scale concatenation cDNA sequencing.";
Genome Res. 7:353-358(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, Eye, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 20-30; 80-97 AND 118-142, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
INTERACTION WITH HERC1.
PubMed=8861955;
Rosa J.L., Casaroli-Marano R.P., Buckler A.J., Vilaro S., Barbacid M.;
"p619, a giant protein related to the chromosome condensation
regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab
proteins.";
EMBO J. 15:4262-4273(1996).
[11]
INTERACTION WITH ASAP2.
PubMed=10022920; DOI=10.1128/MCB.19.3.2338;
Andreev J., Simon J.-P., Sabatini D.D., Kam J., Plowman G.,
Randazzo P.A., Schlessinger J.;
"Identification of a new Pyk2 target protein with Arf-GAP activity.";
Mol. Cell. Biol. 19:2338-2350(1999).
[12]
INTERACTION WITH GGA1; GGA2 AND GGA3.
PubMed=11950392; DOI=10.1042/BJ20020428;
Takatsu H., Yoshino K., Toda K., Nakayama K.;
"GGA proteins associate with Golgi membranes through interaction
between their GGAH domains and ADP-ribosylation factors.";
Biochem. J. 365:369-378(2002).
[13]
INTERACTION WITH PLEKHA8.
PubMed=15107860; DOI=10.1038/ncb1119;
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.;
"FAPPs control Golgi-to-cell-surface membrane traffic by binding to
ARF and PtdIns(4)P.";
Nat. Cell Biol. 6:393-404(2004).
[14]
INTERACTION WITH ARHGAP21.
PubMed=17347647; DOI=10.1038/sj.emboj.7601634;
Menetrey J., Perderiset M., Cicolari J., Dubois T., Elkhatib N.,
El Khadali F., Franco M., Chavrier P., Houdusse A.;
"Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi
membranes.";
EMBO J. 26:1953-1962(2007).
[15]
INTERACTION WITH PI4KB AND NCS1, AND SUBCELLULAR LOCATION.
PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x;
Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.;
"Specificity, promiscuity and localization of ARF protein interactions
with NCS-1 and phosphatidylinositol-4 kinase-III beta.";
Traffic 8:1080-1092(2007).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
MYRISTOYLATION AT GLY-2.
PubMed=20213681; DOI=10.1002/pmic.200900783;
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
Tsunasawa S., Utsumi T.;
"Strategy for comprehensive identification of human N-myristoylated
proteins using an insect cell-free protein synthesis system.";
Proteomics 10:1780-1793(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
INTERACTION WITH PLEKHA3.
PubMed=21454700; DOI=10.1074/jbc.M111.233015;
He J., Scott J.L., Heroux A., Roy S., Lenoir M., Overduin M.,
Stahelin R.V., Kutateladze T.G.;
"Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase
recognition by the FAPP1 pleckstrin homology (PH) domain.";
J. Biol. Chem. 286:18650-18657(2011).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[21]
MYRISTOYLATION AT GLY-2, AND DEMYRISTOYLATION.
PubMed=23535599; DOI=10.1038/nature12004;
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.;
"Proteolytic elimination of N-myristoyl modifications by the Shigella
virulence factor IpaJ.";
Nature 496:106-109(2013).
[22]
INTERACTION WITH PICK1 AND GRIA2.
PubMed=23889934; DOI=10.1016/j.neuron.2013.05.003;
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.;
"The small GTPase Arf1 modulates Arp2/3-mediated actin polymerization
via PICK1 to regulate synaptic plasticity.";
Neuron 79:293-307(2013).
[23]
INTERACTION WITH IQSEC1.
PubMed=24058294; DOI=10.1371/journal.pbio.1001652;
Aizel K., Biou V., Navaza J., Duarte L.V., Campanacci V., Cherfils J.,
Zeghouf M.;
"Integrated conformational and lipid-sensing regulation of endosomal
ArfGEF BRAG2.";
PLoS Biol. 11:E1001652-E1001652(2013).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
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.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[26]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25807930; DOI=10.1002/anie.201500342;
Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J.,
Magee A.I., Tate E.W.;
"Multifunctional reagents for quantitative proteome-wide analysis of
protein modification in human cells and dynamic profiling of protein
lipidation during vertebrate development.";
Angew. Chem. Int. Ed. 54:5948-5951(2015).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[28]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH GDP.
PubMed=7990966; DOI=10.1038/372704a0;
Amor J.C., Harrison D.H., Kahn R.A., Ringe D.;
"Structure of the human ADP-ribosylation factor 1 complexed with
GDP.";
Nature 372:704-708(1994).
[29]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RAT ARFGAP1
CATALYTIC DOMAIN.
PubMed=10102276; DOI=10.1016/S0092-8674(00)80598-X;
Goldberg J.;
"Structural and functional analysis of the ARF1-ARFGAP complex reveals
a role for coatomer in GTP hydrolysis.";
Cell 96:893-902(1999).
[30]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-181 IN COMPLEX WITH GDP;
BREFELDIN AND YEAST GEA1.
PubMed=14690595; DOI=10.1016/S1097-2765(03)00475-1;
Mossessova E., Corpina R.A., Goldberg J.;
"Crystal structure of ARF1*Sec7 complexed with brefeldin A and its
implications for the guanine nucleotide exchange mechanism.";
Mol. Cell 12:1403-1411(2003).
[31]
STRUCTURE BY NMR OF 18-181 IN COMPLEX WITH GDP.
PubMed=15308674; DOI=10.1074/jbc.M402109200;
Seidel R.D., Amor J.C., Kahn R.A., Prestegard J.H.;
"Conformational changes in human Arf1 on nucleotide exchange and
deletion of membrane-binding elements.";
J. Biol. Chem. 279:48307-48318(2004).
[32]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 11-181 IN COMPLEX WITH GDP.
Structural genomics consortium (SGC).;
"Crystal structure of ARFGAP1-ARF1 fusion protein.";
Submitted (JUL-2010) to the PDB data bank.
-!- FUNCTION: GTP-binding protein 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).
-!- FUNCTION: (Microbial infection) Functions as an allosteric
activator of the cholera toxin catalytic subunit, an ADP-
ribosyltransferase. {ECO:0000305}.
-!- SUBUNIT: Interacts (when activated) with GGA1, GGA2 and GGA3; the
interaction is required for proper subcellular location of GGA1,
GGA2 and GGA3 (PubMed:11950392). Interacts with ARHGAP21, ASAP2,
HERC1, PRKCABP, PIP5K1B, TMED2, PSCD2, TMED10 and GRIA2
(PubMed:10022920, PubMed:17347647, PubMed:23889934,
PubMed:8861955). Interacts with ARFGAP1, which hydrolyzes GTP and
thus, regulates its function (PubMed:10102276). Interacts with
PI4KB in the Golgi complex (PubMed:17555535). Interacts with
NCS1/FREQ in the Golgi and at the plasma membrane
(PubMed:17555535). Interacts with PLEKHA3 (PubMed:21454700).
Interacts with PLEKHA8; the interaction, together with
phosphatidylinositol 4-phosphate binding, is required for FAPP2-
mediated glucosylceramide transfer activity (PubMed:15107860).
Interacts (activated) with PICK1 (via PDZ domain); the interaction
blocks Arp2/3 complex inhibition (PubMed:23889934). Interacts with
IQSEC1 (PubMed:24058294). Interacts with C9orf72 (By similarity)
(PubMed:24058294). {ECO:0000250|UniProtKB:P84078,
ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:10102276,
ECO:0000269|PubMed:11950392, ECO:0000269|PubMed:15107860,
ECO:0000269|PubMed:17347647, ECO:0000269|PubMed:17555535,
ECO:0000269|PubMed:21454700, ECO:0000269|PubMed:23889934,
ECO:0000269|PubMed:24058294, ECO:0000269|PubMed:8861955}.
-!- INTERACTION:
Q99418:CYTH2; NbExp=5; IntAct=EBI-447171, EBI-448974;
O60271:SPAG9; NbExp=3; IntAct=EBI-447171, EBI-1023301;
-!- SUBCELLULAR LOCATION: Golgi apparatus
{ECO:0000269|PubMed:17555535}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:17555535}. Cell junction, synapse, synaptosome
{ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane,
postsynaptic density {ECO:0000250}. Membrane {ECO:0000305}; Lipid-
anchor {ECO:0000305}. Golgi apparatus, trans-Golgi network
membrane {ECO:0000250|UniProtKB:P84078}; Lipid-anchor
{ECO:0000250|UniProtKB:P84078}.
-!- PTM: Demyristoylated by S.flexneri cysteine protease IpaJ which
cleaves the peptide bond between N-myristoylated Gly-2 and Asn-3.
{ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:23535599}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
{ECO:0000305}.
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EMBL; M36340; AAA35552.1; -; mRNA.
EMBL; M84326; AAA35512.1; -; mRNA.
EMBL; AF052179; AAC28623.1; -; mRNA.
EMBL; AF055002; AAC09356.1; -; mRNA.
EMBL; AF493881; AAM12595.1; -; mRNA.
EMBL; BT007393; AAP36057.1; -; mRNA.
EMBL; AL136379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC009247; AAH09247.1; -; mRNA.
EMBL; BC010429; AAH10429.1; -; mRNA.
EMBL; BC011358; AAH11358.1; -; mRNA.
EMBL; M84332; AAA35511.1; -; Genomic_DNA.
CCDS; CCDS1565.1; -.
PIR; B40187; A33283.
RefSeq; NP_001019397.1; NM_001024226.1.
RefSeq; NP_001019398.1; NM_001024227.1.
RefSeq; NP_001019399.1; NM_001024228.1.
RefSeq; NP_001649.1; NM_001658.3.
UniGene; Hs.286221; -.
PDB; 1HUR; X-ray; 2.00 A; A/B=2-181.
PDB; 1RE0; X-ray; 2.40 A; A=18-181.
PDB; 1U81; NMR; -; A=18-181.
PDB; 3O47; X-ray; 2.80 A; A/B=11-181.
PDB; 4HMY; X-ray; 7.00 A; C=17-181.
PDB; 6CM9; EM; 3.73 A; C/H=17-181.
PDB; 6CRI; EM; 6.80 A; C/H/K/L/U/V=17-181.
PDB; 6D83; EM; 4.27 A; C/H=17-181.
PDB; 6D84; EM; 6.72 A; C/H/I/N=17-181.
PDB; 6DFF; EM; 3.90 A; C/H=17-181.
PDB; 6FAE; X-ray; 2.35 A; B=18-181.
PDBsum; 1HUR; -.
PDBsum; 1RE0; -.
PDBsum; 1U81; -.
PDBsum; 3O47; -.
PDBsum; 4HMY; -.
PDBsum; 6CM9; -.
PDBsum; 6CRI; -.
PDBsum; 6D83; -.
PDBsum; 6D84; -.
PDBsum; 6DFF; -.
PDBsum; 6FAE; -.
ProteinModelPortal; P84077; -.
SMR; P84077; -.
BioGrid; 106870; 99.
CORUM; P84077; -.
DIP; DIP-31597N; -.
ELM; P84077; -.
IntAct; P84077; 41.
MINT; P84077; -.
STRING; 9606.ENSP00000272102; -.
BindingDB; P84077; -.
ChEMBL; CHEMBL5985; -.
DrugBank; DB04077; Glycerol.
DrugBank; DB04121; Guanosine-3'-Monophosphate-5'-Diphosphate.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
DrugBank; DB04137; Guanosine-5'-Triphosphate.
DrugBank; DB08231; MYRISTIC ACID.
iPTMnet; P84077; -.
PhosphoSitePlus; P84077; -.
SwissPalm; P84077; -.
BioMuta; ARF1; -.
DMDM; 51316985; -.
EPD; P84077; -.
MaxQB; P84077; -.
PaxDb; P84077; -.
PeptideAtlas; P84077; -.
PRIDE; P84077; -.
ProteomicsDB; 57747; -.
TopDownProteomics; P84077; -.
DNASU; 375; -.
Ensembl; ENST00000272102; ENSP00000272102; ENSG00000143761.
Ensembl; ENST00000540651; ENSP00000442980; ENSG00000143761.
Ensembl; ENST00000541182; ENSP00000440005; ENSG00000143761.
GeneID; 375; -.
KEGG; hsa:375; -.
UCSC; uc001hrr.4; human.
CTD; 375; -.
DisGeNET; 375; -.
EuPathDB; HostDB:ENSG00000143761.13; -.
GeneCards; ARF1; -.
H-InvDB; HIX0116279; -.
HGNC; HGNC:652; ARF1.
HPA; CAB007742; -.
MIM; 103180; gene.
neXtProt; NX_P84077; -.
OpenTargets; ENSG00000143761; -.
PharmGKB; PA24934; -.
eggNOG; KOG0070; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00940000153538; -.
HOGENOM; HOG000163691; -.
HOVERGEN; HBG002073; -.
InParanoid; P84077; -.
KO; K07937; -.
OMA; HYYSNTD; -.
OrthoDB; EOG091G0S7S; -.
PhylomeDB; P84077; -.
TreeFam; TF300808; -.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane.
Reactome; R-HSA-167590; Nef Mediated CD4 Down-regulation.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-421837; Clathrin derived vesicle budding.
Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-6811438; Intra-Golgi traffic.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
ChiTaRS; ARF1; human.
EvolutionaryTrace; P84077; -.
GeneWiki; ARF1; -.
GenomeRNAi; 375; -.
PRO; PR:P84077; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143761; Expressed in 230 organ(s), highest expression level in testis.
CleanEx; HS_ARF1; -.
ExpressionAtlas; P84077; baseline and differential.
Genevisible; P84077; HS.
GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
GO; GO:0030137; C:COPI-coated vesicle; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005770; C:late endosome; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
GO; GO:0030017; C:sarcomere; IEA:Ensembl.
GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
GO; GO:0019003; F:GDP binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IBA:GO_Central.
GO; GO:0003924; F:GTPase activity; TAS:Reactome.
GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
GO; GO:1990583; F:phospholipase D activator activity; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0046982; F:protein heterodimerization activity; IMP:CAFA.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0006878; P:cellular copper ion homeostasis; IMP:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
GO; GO:0097061; P:dendritic spine organization; ISS:UniProtKB.
GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
GO; GO:0055108; P:Golgi to transport vesicle transport; IEA:Ensembl.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0060292; P:long-term synaptic depression; ISS:UniProtKB.
GO; GO:0097212; P:lysosomal membrane organization; IEA:Ensembl.
GO; GO:1990386; P:mitotic cleavage furrow ingression; IEA:Ensembl.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IEA:Ensembl.
GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IEA:Ensembl.
GO; GO:1902824; P:positive regulation of late endosome to lysosome transport; IEA:Ensembl.
GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
GO; GO:1902307; P:positive regulation of sodium ion transmembrane transport; IEA:Ensembl.
GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IEA:Ensembl.
GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
GO; GO:1903725; P:regulation of phospholipid metabolic process; IEA:Ensembl.
GO; GO:0002090; P:regulation of receptor internalization; ISS:UniProtKB.
GO; GO:0070142; P:synaptic vesicle budding; IEA:Ensembl.
GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IEA:Ensembl.
GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR006689; Small_GTPase_ARF/SAR.
Pfam; PF00025; Arf; 1.
PRINTS; PR00328; SAR1GTPBP.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51417; ARF; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell junction; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing;
ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
Membrane; Myristate; Nucleotide-binding; Postsynaptic cell membrane;
Protein transport; Reference proteome; Synapse; Synaptosome;
Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930}.
CHAIN 2 181 ADP-ribosylation factor 1.
/FTId=PRO_0000207378.
NP_BIND 24 32 GTP. {ECO:0000244|PDB:1HUR, ECO:0000305}.
NP_BIND 126 129 GTP. {ECO:0000244|PDB:1HUR,
ECO:0000244|PDB:1RE0,
ECO:0000244|PDB:1U81,
ECO:0000244|PDB:3O47, ECO:0000305}.
BINDING 160 160 GTP; via amide nitrogen.
{ECO:0000244|PDB:1HUR,
ECO:0000244|PDB:1RE0,
ECO:0000244|PDB:3O47}.
MOD_RES 2 2 N-acetylglycine; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
LIPID 2 2 N-myristoyl glycine; alternate.
{ECO:0000269|PubMed:20213681,
ECO:0000269|PubMed:23535599,
ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930}.
HELIX 6 9 {ECO:0000244|PDB:1HUR}.
STRAND 10 12 {ECO:0000244|PDB:1HUR}.
STRAND 14 16 {ECO:0000244|PDB:1HUR}.
STRAND 19 25 {ECO:0000244|PDB:1HUR}.
HELIX 30 36 {ECO:0000244|PDB:1HUR}.
STRAND 42 45 {ECO:0000244|PDB:1HUR}.
STRAND 49 51 {ECO:0000244|PDB:6FAE}.
STRAND 53 58 {ECO:0000244|PDB:1HUR}.
STRAND 61 67 {ECO:0000244|PDB:1HUR}.
TURN 72 74 {ECO:0000244|PDB:6FAE}.
HELIX 75 78 {ECO:0000244|PDB:6FAE}.
HELIX 79 82 {ECO:0000244|PDB:1HUR}.
STRAND 85 93 {ECO:0000244|PDB:1HUR}.
HELIX 97 99 {ECO:0000244|PDB:6FAE}.
HELIX 100 111 {ECO:0000244|PDB:1HUR}.
HELIX 114 116 {ECO:0000244|PDB:1HUR}.
STRAND 120 126 {ECO:0000244|PDB:1HUR}.
STRAND 131 134 {ECO:0000244|PDB:1U81}.
HELIX 136 143 {ECO:0000244|PDB:1HUR}.
HELIX 145 147 {ECO:0000244|PDB:1HUR}.
STRAND 153 157 {ECO:0000244|PDB:1HUR}.
TURN 160 163 {ECO:0000244|PDB:1HUR}.
HELIX 166 179 {ECO:0000244|PDB:1HUR}.
SEQUENCE 181 AA; 20697 MW; AAC773D4A60186B6 CRC64;
MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV
LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ
K


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