P84077 (ARF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ADP-ribosylation factor 1

Gene names

Name:

ARF1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Interacts with PRKCABP, GGA1, ASAP2 and PIP5K1B By similarity. Interacts with ARFGAP1, which hydrolyzes GTP and thus, regulates its function. Binds ASAP2. Interacts with HERC1 and ARHGAP21. Interacts with PI4KB in the Golgi complex. Interacts with NCS1/FREQ in the Golgi and at the plasma membrane. This interaction at the plasm membrane requires a myristoylated NCS1/FREQ. Interacts with TMED2 and TMED10. Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Golgi apparatus. Cytoplasm › perinuclear region Ref.13.
Sequence similarities	Belongs to the small GTPase superfamily. Arf family.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Cytoplasm Golgi apparatus
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	COPI coating of Golgi vesicle Traceable author statement. Source: Reactome cellular copper ion homeostasis Inferred from mutant phenotype. Source: UniProtKB post-Golgi vesicle-mediated transport Traceable author statement. Source: Reactome protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of defense response to virus by virus Traceable author statement. Source: Reactome retrograde vesicle-mediated transport, Golgi to ER Traceable author statement. Source: Reactome small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro viral reproduction Traceable author statement. Source: Reactome
Cellular component	Golgi membrane Traceable author statement. Source: Reactome cytosol Traceable author statement. Source: Reactome perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Traceable author statement. Source: ProtInc
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct receptor signaling protein activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CYTH2	Q99418	4	EBI-447171,EBI-448974

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 181

180

ADP-ribosylation factor 1

PRO_0000207378

Regions

Nucleotide binding

24 – 31

8

GTP By similarity

Nucleotide binding

126 – 129

4

GTP By similarity

Amino acid modifications

Modified residue

147

1

Phosphoserine Ref.14

Lipidation

2

1

N-myristoyl glycine Ref.15

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

181

Helix Strand Turn

Details...

Helix

6 – 9

4

Beta strand

10 – 12

3

Beta strand

14 – 16

3

Beta strand

19 – 25

7

Helix

30 – 36

7

Beta strand

42 – 45

4

Beta strand

53 – 58

6

Beta strand

61 – 67

7

Helix

79 – 82

4

Beta strand

85 – 93

9

Helix

100 – 111

12

Helix

114 – 116

3

Beta strand

120 – 126

7

Helix

136 – 143

8

Helix

145 – 147

3

Beta strand

153 – 157

5

Turn

160 – 163

4

Helix

166 – 179

14

Sequences

	Sequence		Length	Mass (Da)
	P84077 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: AAC773D4A60186B6	FASTA	181	20,697
	10 20 30 40 50 60 MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN 70 80 90 100 110 120 ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV 130 140 150 160 170 180 LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2474826] [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: 1899243] [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: 1577740] [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: 9110174] [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: 16710414] [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: 15489334] [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, 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: 8861955] [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: 10022920] [Abstract] Cited for: INTERACTION WITH ASAP2.
[12]	"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: 17347647] [Abstract] Cited for: INTERACTION WITH ARHGAP21.
[13]	"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: 17555535] [Abstract] Cited for: INTERACTION WITH PI4KB AND NCS1, SUBCELLULAR LOCATION.
[14]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 20213681] [Abstract] Cited for: MYRISTOYLATION AT GLY-2.
[16]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"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: 7990966] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[18]	"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: 10102276] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF COMPLEX WITH RAT ARFGAP1 CATALYTIC DOMAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00215914.

PIR

A33283. B40187.

RefSeq

NP_001019397.1. NM_001024226.1.
NP_001019398.1. NM_001024227.1.
NP_001019399.1. NM_001024228.1.
NP_001649.1. NM_001658.3.

UniGene

Hs.286221.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HUR	X-ray	2.00	A/B	2-181	[»]
1RE0	X-ray	2.40	A	18-181	[»]
1U81	NMR	-	A	18-180	[»]
3O47	X-ray	2.80	A/B	11-181	[»]

ProteinModelPortal

P84077.

SMR

P84077. Positions 2-180.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31597N.

IntAct

P84077. 23 interactions.

MINT

MINT-4999599.

STRING

P84077.

PTM databases

PhosphoSite

P84077.

Polymorphism databases

DMDM

51316985.

Proteomic databases

PeptideAtlas

P84077.

PRIDE

P84077.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000272102; ENSP00000272102; ENSG00000143761.

GeneID

375.

KEGG

hsa:375.

UCSC

uc001hrr.1. human.

Organism-specific databases

CTD

375.

GeneCards

GC01P228270.

H-InvDB

HIX0001656.

HGNC

HGNC:652. ARF1.

HPA

CAB007742.

MIM

103180. gene.

neXtProt

NX_P84077.

PharmGKB

PA24934.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09478.

GeneTree

ENSGT00570000078761.

HOGENOM

HBG745225.

HOVERGEN

HBG002073.

InParanoid

P84077.

OMA

NDRDRMR.

OrthoDB

EOG4PZJ7Q.

PhylomeDB

P84077.

Enzyme and pathway databases

Pathway_Interaction_DB

arf_3pathway. Arf1 pathway.
arf6downstreampathway. Arf6 downstream pathway.
pi3kcipathway. Class I PI3K signaling events.

Reactome

REACT_11123. Membrane Trafficking.
REACT_6185. HIV Infection.

Gene expression databases

ArrayExpress

P84077.

Bgee

P84077.

CleanEx

HS_ARF1.

Genevestigator

P84077.

GermOnline

ENSG00000143761. Homo sapiens.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]

KO

K07937.

PANTHER

PTHR11711. ARF/SAR. 1 hit.

Pfam

PF00025. Arf. 1 hit.
[Graphical view]

PRINTS

PR00328. SAR1GTPBP.

SMART

SM00177. ARF. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. Small_GTP. 1 hit.

PROSITE

PS51417. ARF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

1569.

SOURCE

Search...

Entry information

Entry name

ARF1_HUMAN

Accession

Primary (citable) accession number: P84077
Secondary accession number(s): P10947, P32889

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 96 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.