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P18085 (ARF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ADP-ribosylation factor 4
Gene names
Name:ARF4
Synonyms:ARF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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; may modulate vesicle budding and uncoating within the Golgi apparatus.

Subcellular location

Golgi apparatus.

Sequence similarities

Belongs to the small GTPase superfamily. Arf family.

Caution

Was originally thought to be ARF2.

Ontologies

Keywords
   Biological processER-Golgi transport
Protein transport
Transport
   Cellular componentGolgi apparatus
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Myristate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of phospholipase D activity

Inferred from direct assay PubMed 12446727. Source: UniProt

brain development

Inferred from electronic annotation. Source: Ensembl

cell migration

Inferred from direct assay PubMed 22004728. Source: UniProt

epidermal growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from direct assay PubMed 19041174. Source: UniProt

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12446727. Source: UniProt

protein ADP-ribosylation

Inferred from direct assay Ref.2. Source: UniProt

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of reactive oxygen species metabolic process

Inferred from direct assay PubMed 19041174. Source: UniProt

response to axon injury

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

vesicle-mediated transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay PubMed 12446727. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

ruffle membrane

Inferred from direct assay PubMed 12446727. Source: UniProt

   Molecular_functionGTP binding

Inferred from direct assay PubMed 12446727. Source: UniProt

epidermal growth factor receptor binding

Inferred from direct assay PubMed 12446727. Source: UniProt

protein binding

Inferred from physical interaction PubMed 21988832. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RCHY1Q96PM53EBI-1237085,EBI-947779

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 180179ADP-ribosylation factor 4
PRO_0000207391

Regions

Nucleotide binding24 – 318GTP
Nucleotide binding67 – 715GTP
Nucleotide binding126 – 1294GTP

Amino acid modifications

Lipidation21N-myristoyl glycine Potential

Natural variations

Natural variant681V → A.
Corresponds to variant rs11550597 [ dbSNP | Ensembl ].
VAR_048317

Secondary structure

....................................... 180
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18085 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3A43EB1F37A81BD9

FASTA18020,511
        10         20         30         40         50         60 
MGLTISSLFS RLFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN 

        70         80         90        100        110        120 
ICFTVWDVGG QDRIRPLWKH YFQNTQGLIF VVDSNDRERI QEVADELQKM LLVDELRDAV 

       130        140        150        160        170        180 
LLLFANKQDL PNAMAISEMT DKLGLQSLRN RTWYVQATCA TQGTGLYEGL DWLSNELSKR 

« Hide

References

« Hide 'large scale' references
[1]"Selective amplification of an mRNA and related pseudogene for a human ADP-ribosylation factor, a guanine nucleotide-dependent protein activator of cholera toxin."
Monaco L., Murtagh J.J. Jr., Newman K.B., Tsai S.-C., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 87:2206-2210(1990) [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]"Cloning and characterization of the human ADP-ribosylation factor 4 gene."
Lebeda R.A., Haun R.S.
Gene 237:209-214(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[6]"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: Bone marrow, Placenta, Skin and Urinary bladder.
[7]"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].
[8]"Structure of human ADP-ribosylation factor 4."
Structural genomics consortium (SGC)
Submitted (APR-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH GDP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36341 mRNA. Translation: AAA53081.1.
AF104238 expand/collapse EMBL AC list , AF104233, AF104234, AF104235, AF104236, AF104237 Genomic DNA. Translation: AAD54674.1.
AF493883 mRNA. Translation: AAM12597.1.
AK313008 mRNA. Translation: BAG35844.1.
BC003364 mRNA. Translation: AAH03364.1.
BC008753 mRNA. Translation: AAH08753.1.
BC016325 mRNA. Translation: AAH16325.1.
BC022866 mRNA. Translation: AAH22866.1.
CCDSCCDS2884.1.
PIRB38622.
RefSeqNP_001651.1. NM_001660.3.
UniGeneHs.652183.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z6XX-ray2.70A/B1-180[»]
ProteinModelPortalP18085.
SMRP18085. Positions 4-178.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106873. 21 interactions.
IntActP18085. 7 interactions.
MINTMINT-2801449.
STRING9606.ENSP00000306010.

PTM databases

PhosphoSiteP18085.

Polymorphism databases

DMDM114123.

Proteomic databases

MaxQBP18085.
PaxDbP18085.
PRIDEP18085.

Protocols and materials databases

DNASU378.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303436; ENSP00000306010; ENSG00000168374.
GeneID378.
KEGGhsa:378.
UCSCuc003dix.4. human.

Organism-specific databases

CTD378.
GeneCardsGC03M057532.
HGNCHGNC:655. ARF4.
MIM601177. gene.
neXtProtNX_P18085.
PharmGKBPA24937.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000163691.
HOVERGENHBG002073.
InParanoidP18085.
KOK07939.
OMAGADELQK.
OrthoDBEOG77WWDV.
PhylomeDBP18085.
TreeFamTF300808.

Gene expression databases

ArrayExpressP18085.
BgeeP18085.
CleanExHS_ARF4.
GenevestigatorP18085.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
PfamPF00025. Arf. 1 hit.
[Graphical view]
PRINTSPR00328. SAR1GTPBP.
SMARTSM00177. ARF. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51417. ARF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARF4. human.
EvolutionaryTraceP18085.
GeneWikiARF4.
GenomeRNAi378.
NextBio1583.
PROP18085.
SOURCESearch...

Entry information

Entry nameARF4_HUMAN
AccessionPrimary (citable) accession number: P18085
Secondary accession number(s): B2R7J7, P21371
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM