Q8N6T3 (ARFG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Protein existence	Evidence 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 TMED2. 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 TMED2. The interaction with TMED2 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 BAB55009.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB55113.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAB70901.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Cytoplasm Golgi apparatus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	GTPase activation
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	COPI coating of Golgi vesicle Traceable author statement. Source: Reactome activation of signaling protein activity involved in unfolded protein response Traceable author statement. Source: Reactome cellular protein metabolic process Traceable author statement. Source: Reactome protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of ARF GTPase activity Inferred from electronic annotation. Source: InterPro retrograde vesicle-mediated transport, Golgi to ER Traceable author statement. Source: Reactome
Cellular_component	Golgi-associated vesicle membrane Traceable author statement. Source: Reactome cytosol Traceable author statement. Source: Reactome endoplasmic reticulum Inferred from direct assay. Source: HPA nuclear membrane Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA synapse Inferred from electronic annotation. Source: Compara
Molecular_function	ARF GTPase activator activity Inferred from electronic annotation. Source: InterPro GTPase activator activity Inferred from direct assay PubMed 22423108. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LRRK2	Q5S007	6	EBI-6288865,EBI-5323863

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...AVWTTSKTAT

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 406

406

ADP-ribosylation factor GTPase-activating protein 1

PRO_0000074190

Regions

Domain

7 – 124

118

Arf-GAP

Zinc finger

22 – 45

24

C4-type

Amino acid modifications

Modified residue

135

1

Phosphothreonine Ref.8 Ref.11

Modified residue

189

1

Phosphothreonine Ref.7 Ref.9 Ref.11

Modified residue

231

1

N6-acetyllysine Ref.10

Modified residue

304

1

Phosphoserine Ref.8

Modified residue

343

1

Phosphoserine By similarity

Modified residue

345

1

Phosphoserine By similarity

Modified residue

348

1

Phosphoserine By similarity

Modified residue

361

1

Phosphoserine By similarity

Natural variations

Alternative sequence

239

1

K → KFWGHKQQPEP in isoform 2.

VSP_000298

Alternative sequence

279 – 406

128

VQGVG…DNQNW → CQRRLCCHQSHCSAGHLGRA FCPVSWHEALCGQTGREEQA SLLPPKHVVGALEVCARGCP RCHVPHTPGTAAEWPGRLCL SRESVVRDGGTSPPFFRGKQ RAPWTAPRRATVIRTAVWTT SKTAT in isoform 3.

VSP_021818

Alternative sequence

279 – 280

2

Missing in isoform 2.

VSP_000299

Natural variant

184

1

V → M.
Corresponds to variant rs2273499 [ dbSNP | Ensembl ].

VAR_015187

Experimental info

Sequence conflict

274

1

Q → R in BAB55009. Ref.1

Secondary structure

1

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406

Helix Strand Turn

Details...

Helix

4 – 14

11

Turn

17 – 20

4

Turn

23 – 25

3

Beta strand

32 – 34

3

Turn

35 – 38

4

Beta strand

39 – 41

3

Helix

43 – 52

10

Turn

54 – 56

3

Beta strand

59 – 62

4

Helix

69 – 77

9

Helix

80 – 88

9

Helix

99 – 103

5

Helix

106 – 119

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 27, 2003. Version 2. Checksum: CAE41828DE660621	FASTA	406	44,668
	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
	Isoform 2 [UniParc]. Checksum: BD081C6CE6CF0A18	FASTA	414	45,676
	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 KFGSQASQKF 250 260 270 280 290 300 WGHKQQPEPA SELGHSLNEN VLKPAQEKVK EGKIFDDVSS GVSQLASKGV GSKGWRDVTT 310 320 330 340 350 360 FFSGKAEGPL DSPSEGHSYQ NSGLDHFQNS NIDQSFWETF GSAEPTKTRK SPSSDSWTCA 370 380 390 400 410 DTSTERRSSD SWEVWGSAST NRNSNSDGGE GGEGTKKAVP PAVPTDDGWD NQNW
	Isoform 3 [UniParc]. Checksum: 0C695741E21D0F6F	FASTA	403	44,467
	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 GVSQLASKCQ RRLCCHQSHC SAGHLGRAFC 310 320 330 340 350 360 PVSWHEALCG QTGREEQASL LPPKHVVGAL EVCARGCPRC HVPHTPGTAA EWPGRLCLSR 370 380 390 400 ESVVRDGGTS PPFFRGKQRA PWTAPRRATV IRTAVWTTSK TAT

References

	« Hide 'large scale' referencesShow '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. , 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] (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. , 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] [Europe PMC] [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. , 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] [Europe PMC] [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] [Europe PMC] [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 (ISOFORM 1). Tissue: Fetal brain.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135 AND SER-304, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-231, MASS SPECTROMETRY.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135 AND THR-189, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"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

EMBL
GenBank
DDBJ

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.
CH471077 Genomic DNA. Translation: EAW75294.1.
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.

IPI

IPI00175169.
IPI00217354.
IPI00449160.

PIR

T46298.

RefSeq

NP_060679.1. NM_018209.2.
NP_783202.1. NM_175609.1.

UniGene

Hs.25584.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DWD	X-ray	2.40	A/B	1-128	[»]
3O47	X-ray	2.80	A/B	1-140	[»]

ProteinModelPortal

Q8N6T3.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8N6T3. 16 interactions.

MINT

MINT-1409968.

STRING

9606.ENSP00000314615.

PTM databases

PhosphoSite

Q8N6T3.

Polymorphism databases

DMDM

27923731.

Proteomic databases

PaxDb

Q8N6T3.

PRIDE

Q8N6T3.

Protocols and materials databases

DNASU

55738.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000353546; ENSP00000314615; ENSG00000101199.
ENST00000370275; ENSP00000359298; ENSG00000101199.
ENST00000370283; ENSP00000359306; ENSG00000101199.

GeneID

55738.

KEGG

hsa:55738.

UCSC

uc002yel.3. human.
uc002yem.3. human.

Organism-specific databases

CTD

55738.

GeneCards

GC20P061904.

H-InvDB

HIX0174713.

HGNC

HGNC:15852. ARFGAP1.

HPA

HPA051019.

MIM

608377. gene.

neXtProt

NX_Q8N6T3.

PharmGKB

PA164741246.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5347.

HOVERGEN

HBG050562.

KO

K12492.

OMA

SDSWENW.

OrthoDB

EOG4M65HQ.

Enzyme and pathway databases

Pathway_Interaction_DB

arf_3pathway. Arf1 pathway.

Reactome

REACT_11123. Membrane Trafficking.
REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q8N6T3.

Bgee

Q8N6T3.

CleanEx

HS_ARFGAP1.

Genevestigator

Q8N6T3.

GermOnline

ENSG00000101199. Homo sapiens.

Family and domain databases

InterPro

IPR001164. ArfGAP.
[Graphical view]

Pfam

PF01412. ArfGap. 1 hit.
[Graphical view]

PRINTS

PR00405. REVINTRACTNG.

SMART

SM00105. ArfGap. 1 hit.
[Graphical view]

PROSITE

PS50115. ARFGAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ARFGAP1. human.

EvolutionaryTrace

Q8N6T3.

GenomeRNAi

55738.

NextBio

60684.

SOURCE

Search...

Entry information

Entry name

ARFG1_HUMAN

Accession

Primary (citable) accession number: Q8N6T3
Secondary accession number(s): B7ZBI3 , E1P5I9, Q6PK71, Q96KC4, Q96T02, Q9NSU3, Q9NVF6, Q9UIL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	January 27, 2003
Last modified:	May 29, 2013
This is version 112 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.