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Reviewed, UniProtKB/Swiss-Prot Q8N6T3 (ARFG1_HUMAN)

Last modified November 24, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ADP-ribosylation factor GTPase-activating protein 1
      Short name=ARF GAP 1
Alternative name(s):
    ADP-ribosylation factor 1 GTPase-activating protein
      Short name=ARF1 GAP
    ARF1-directed GTPase-activating protein
Gene names
Name: ARFGAP1
Synonyms: ARF1GAP
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and RNP24. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine By similarity.

Subunit structure

Interacts with ARF1. Interacts with the COPI coat proteins, KDELR1 and RNP24. The interaction with RNP24 inhibits the GAP activity By similarity.

Subcellular location

Cytoplasm By similarity. Golgi apparatus By similarity. Note: Associates with the Golgi complex By similarity.

Domain

The region downstream of Arf-GAP domain is essential to GAP activity in vivo. This region may be required for its targeting to Golgi membranes By similarity.

Sequence similarities

Contains 1 Arf-GAP domain.

Sequence caution

The sequence CAB70901.1 differs from that shown. Reason: Miscellaneous discrepancy. Intron retention.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N6T3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8N6T3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     239-239: K → KFWGHKQQPEP
     279-280: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8N6T3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     279-406: VQGVGSKGWR...TDDGWDNQNW → CQRRLCCHQS...RATVIRTAVW

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406ADP-ribosylation factor GTPase-activating protein 1
PRO_0000074190

Regions

Domain7 – 124118Arf-GAP
Zinc finger22 – 4524C4-type

Amino acid modifications

Modified residue1351Phosphothreonine Ref.7 Ref.10 Ref.11
Modified residue1891Phosphothreonine Ref.8
Modified residue2311N6-acetyllysine Ref.15
Modified residue2461Phosphoserine Ref.9
Modified residue3041Phosphoserine Ref.11
Modified residue3431Phosphoserine By similarity
Modified residue3451Phosphoserine By similarity
Modified residue3481Phosphoserine By similarity
Modified residue3611Phosphoserine By similarity

Natural variations

Alternative sequence2391K → KFWGHKQQPEP in isoform 2.
VSP_000298
Alternative sequence279 – 406128VQGVG…DNQNW → CQRRLCCHQSHCSAGHLGRA FCPVSWHEALCGQTGREEQA SLLPPKHVVGALEVCARGCP RCHVPHTPGTAAEWPGRLCL SRESVVRDGGTSPPFFRGKQ RAPWTAPRRATVIRTAVW in isoform 3.
VSP_021818
Alternative sequence279 – 2802Missing in isoform 2.
VSP_000299
Natural variant1841V → M: dbSNP rs2273499.
VAR_015187

Experimental info

Sequence conflict2741Q → R in BAB55009. Ref.1

Secondary structure

................... 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 27, 2003. Version 2.
Checksum: CAE41828DE660621

FASTA40644,668
        10         20         30         40         50         60 
MASPRTRKVL KEVRVQDENN VCFECGAFNP QWVSVTYGIW ICLECSGRHR GLGVHLSFVR 

        70         80         90        100        110        120 
SVTMDKWKDI ELEKMKAGGN AKFREFLESQ EDYDPCWSLQ EKYNSRAAAL FRDKVVALAE 

       130        140        150        160        170        180 
GREWSLESSP AQNWTPPQPR TLPSMVHRVS GQPQSVTASS DKAFEDWLND DLGSYQGAQG 

       190        200        210        220        230        240 
NRYVGFGNTP PPQKKEDDFL NNAMSSLYSG WSSFTTGASR FASAAKEGAT KFGSQASQKA 

       250        260        270        280        290        300 
SELGHSLNEN VLKPAQEKVK EGKIFDDVSS GVSQLASKVQ GVGSKGWRDV TTFFSGKAEG 

       310        320        330        340        350        360 
PLDSPSEGHS YQNSGLDHFQ NSNIDQSFWE TFGSAEPTKT RKSPSSDSWT CADTSTERRS 

       370        380        390        400 
SDSWEVWGSA STNRNSNSDG GEGGEGTKKA VPPAVPTDDG WDNQNW 

« Hide

Isoform 2.

Checksum: BD081C6CE6CF0A18
Show »

FASTA41445,676
Isoform 3.

Checksum: 2F5D2375FCE61598
Show »

FASTA39643,776

References

« Hide 'large scale' references
[1]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed: 11780052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Brain and Fetal brain.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 240-406 (ISOFORM 1).
Tissue: Testis.
[6]"HRI NTT human fetal brain cDNA project."
Ueki N.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 299-406.
Tissue: Fetal brain.
[7]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, MASS SPECTROMETRY.
[10]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135, MASS SPECTROMETRY.
[11]"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 THR-135 AND SER-304, MASS SPECTROMETRY.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, MASS SPECTROMETRY.
[14]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, MASS SPECTROMETRY.
Tissue: T-cell.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-231, MASS SPECTROMETRY.
[16]"Crystal structure of the ARFGAP domain of human ARFGAP1."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-128 IN COMPLEX WITH ZINC IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

AK001629 mRNA. Translation: BAA91796.1.
AK027268 mRNA. Translation: BAB55009.1. Different initiation.
AK027441 mRNA. Translation: BAB55113.1. Different initiation.
AL121827 Genomic DNA. Translation: CAX12645.1.
CH471077 Genomic DNA. Translation: EAW75292.1.
BC000786 mRNA. Translation: AAH00786.1.
BC006085 mRNA. Translation: AAH06085.1.
BC011876 mRNA. Translation: AAH11876.1.
BC028233 mRNA. Translation: AAH28233.1.
AL137744 mRNA. Translation: CAB70901.1. Sequence problems.
AB015340 mRNA. Translation: BAA88117.1.
IPIIPI00175169.
IPI00217354.
IPI00449160.
PIRT46298.
RefSeqNP_060679.1.
NP_783202.1.
UniGeneHs.25584

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3DWDX-ray2.40A/B1-128[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ8N6T3. 1 interaction.
STRINGQ8N6T3.

PTM databases

PhosphoSiteQ8N6T3.

Proteomic databases

PRIDEQ8N6T3.

Genome annotation databases

EnsemblENST00000370283; ENSP00000359306; ENSG00000101199; Homo sapiens. [Genome view]
GeneID55738.
KEGGhsa:55738.
UCSCuc002yel.1. human.
uc002yem.1. human.
uc002yen.1. human.

Organism-specific databases

CTD55738.
GeneCardsGC20P061374.
H-InvDBHIX0015997.
HGNCHGNC:15852. ARFGAP1.
MIM608377. gene.
PharmGKBPA201060.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ8N6T3.
OMAQASQKFW.

Enzyme and pathway databases

Pathway_Interaction_DBarf_3pathway. Arf1 pathway.
ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressQ8N6T3.
BgeeQ8N6T3.
CleanExHS_ARFGAP1.
GenevestigatorQ8N6T3.
GermOnlineENSG00000101199. Homo sapiens.

Family and domain databases

InterProIPR001164. ArfGAP.
[Graphical view]
PfamPF01412. ArfGap. 1 hit.
[Graphical view]
PRINTSPR00405. REVINTRACTNG.
SMARTSM00105. ArfGap. 1 hit.
[Graphical view]
PROSITEPS50115. ARFGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio60684.
SOURCESearch...

Entry information

Entry nameARFG1_HUMAN
AccessionPrimary (citable) accession number: Q8N6T3
Secondary accession number(s): B7ZBI3 expand/collapse secondary AC list , Q6PK71, Q96KC4, Q96T02, Q9NSU3, Q9NVF6, Q9UIL0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 27, 2003
Last modified: November 24, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents