Q9NP61 (ARFG3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ADP-ribosylation factor GTPase-activating protein 3
Short name=ARF GAP 3

Gene names

Name:	ARFGAP3
Synonyms:	ARFGAP1

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	516 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. Ref.8
Enzyme regulation	GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2). Ref.8
Subcellular location	Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Note: Also found on peripheral punctate structures likely to be endoplasmic reticulum-Golgi intermediate compartment. Ref.11
Tissue specificity	Widely expressed. Highest expression in endocrine glands (pancreas, pituitary gland, salivary gland, and prostate) and testis with a much higher expression in the testis than in the ovary. Ref.1
Developmental stage	Expressed at higher level in adult thymus, brain and lung, than in corresponding fetal tissues. Expressed at lower level in spleen, heart, kidney and liver during development.
Sequence similarities	Contains 1 Arf-GAP domain.
Caution	Was originally (Ref.1) termed ARFGAP1.
Sequence caution	The sequence BAA92076.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB14236.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Cytoplasm Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil 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	intracellular protein transport Non-traceable author statement Ref.8. Source: UniProtKB protein secretion Inferred from expression pattern Ref.8. Source: UniProtKB regulation of ARF GTPase activity Inferred from electronic annotation. Source: InterPro vesicle-mediated transport Non-traceable author statement Ref.8. Source: UniProtKB
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay Ref.8. Source: UniProtKB
Molecular function	ARF GTPase activator activity Inferred from direct assay Ref.8. Source: UniProtKB protein transporter activity Non-traceable author statement Ref.8. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 516

516

ADP-ribosylation factor GTPase-activating protein 3

PRO_0000074193

Regions

Domain

10 – 126

117

Arf-GAP

Zinc finger

25 – 48

24

C4-type

Coiled coil

243 – 263

21

Potential

Compositional bias

348 – 377

30

Ser-rich

Amino acid modifications

Modified residue

143

1

Phosphoserine Ref.9

Modified residue

223

1

N6-acetyllysine Ref.16

Modified residue

228

1

N6-acetyllysine Ref.16

Modified residue

229

1

N6-acetyllysine Ref.16

Modified residue

270

1

Phosphoserine Ref.12

Modified residue

331

1

Phosphoserine Ref.10 Ref.13

Modified residue

370

1

Phosphoserine Ref.15

Modified residue

428

1

Phosphoserine Ref.14

Modified residue

453

1

Phosphoserine Ref.13 Ref.15

Natural variations

Natural variant

231

1

S → G.
Corresponds to variant rs9607957 [ dbSNP | Ensembl ].

VAR_055523

Natural variant

290

1

E → G in a breast cancer sample; somatic mutation. Ref.19

VAR_036177

Natural variant

355

1

S → R. Ref.3 Ref.5 Ref.7
Corresponds to variant rs1018448 [ dbSNP | Ensembl ].

VAR_013447

Natural variant

370

1

S → G.
Corresponds to variant rs16986123 [ dbSNP | Ensembl ].

VAR_055524

Natural variant

468

1

Q → H.
Corresponds to variant rs35498349 [ dbSNP | Ensembl ].

VAR_055525

Natural variant

482

1

A → T.
Corresponds to variant rs36003980 [ dbSNP | Ensembl ].

VAR_055526

Natural variant

490

1

Q → R.
Corresponds to variant rs11551619 [ dbSNP | Ensembl ].

VAR_055527

Experimental info

Sequence conflict

339

1

K → R in BAA92076. Ref.7

Sequence conflict

401

1

T → A in BAA92076. Ref.7

Sequence conflict

458

1

S → P in BAB14236. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

516

Helix Strand Turn

Details...

Helix

6 – 18

13

Turn

20 – 22

3

Beta strand

26 – 28

3

Turn

38 – 41

4

Helix

46 – 55

10

Turn

57 – 59

3

Beta strand

65 – 67

3

Helix

73 – 80

8

Helix

84 – 94

11

Helix

101 – 104

4

Helix

108 – 126

19

Beta strand

129 – 131

3

Sequences

	Sequence		Length	Mass (Da)
	Q9NP61 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: E355E56A5D867F8E	FASTA	516	56,928
	10 20 30 40 50 60 MGDPSKQDIL TIFKRLRSVP TNKVCFDCGA KNPSWASITY GVFLCIDCSG SHRSLGVHLS 70 80 90 100 110 120 FIRSTELDSN WSWFQLRCMQ VGGNASASSF FHQHGCSTND TNAKYNSRAA QLYREKIKSL 130 140 150 160 170 180 ASQATRKHGT DLWLDSCVVP PLSPPPKEED FFASHVSPEV SDTAWASAIA EPSSLTSRPV 190 200 210 220 230 240 ETTLENNEGG QEQGPSVEGL NVPTKATLEV SSIIKKKPNQ AKKGLGAKKG SLGAQKLANT 250 260 270 280 290 300 CFNEIEKQAQ AADKMKEQED LAKVVSKEES IVSSLRLAYK DLEIQMKKDE KMNISGKKNV 310 320 330 340 350 360 DSDRLGMGFG NCRSVISHSV TSDMQTIEQE SPIMAKPRKK YNDDSDDSYF TSSSSYFDEP 370 380 390 400 410 420 VELRSSSFSS WDDSSDSYWK KETSKDTETV LKTTGYSDRP TARRKPDYEP VENTDEAQKK 430 440 450 460 470 480 FGNVKAISSD MYFGRQSQAD YETRARLERL SASSSISSAD LFEEPRKQPA GNYSLSSVLP 490 500 510 NAPDMAQFKQ GVRSVAGKLS VFANGVVTSI QDRYGS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization, chromosomal assignment, and tissue expression of a novel human gene belonging to the ARF GAP family." Zhang C., Yu Y., Zhang S., Liu M., Xing G., Wei H., Bi J., Liu X., Zhou G., Dong C., Hu Z., Zhang Y., Luo L., Wu C., Zhao S., He F. Genomics 63:400-408(2000) [PubMed: 10704287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Placenta.
[2]	"Reevaluating human gene annotation: a second-generation analysis of chromosome 22." Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I. Genome Res. 13:27-36(2003) [PubMed: 12529303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-355.
[4]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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], VARIANT ARG-355. Tissue: Lung.
[6]	"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 44-516. Tissue: Testis.
[7]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-516, VARIANT ARG-355. Tissue: Placenta.
[8]	"Functional characterization of novel human ARFGAP3." Liu X., Zhang C., Xing G., Chen Q., He F. FEBS Lett. 490:79-83(2001) [PubMed: 11172815] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Two human ARFGAPs associated with COP-I-coated vesicles." Frigerio G., Grimsey N., Dale M., Majoul I., Duden R. Traffic 8:1644-1655(2007) [PubMed: 17760859] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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-331 AND SER-453, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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 SER-428, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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 SER-370 AND SER-453, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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-223; LYS-228 AND LYS-229, MASS SPECTROMETRY.
[17]	"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].
[18]	"Solution structure of the ARFGAP domain of ADP-ribosylation factor GTPase-activating protein 3 (ARFGAP 3)." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-136.
[19]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-290.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF111847 mRNA. Translation: AAF40310.1.
AL159143 mRNA. Translation: CAB76901.1.
CR456382 mRNA. Translation: CAG30268.1.
AL049757, AL049758 Genomic DNA. Translation: CAI21510.1.
AL049758, AL049757 Genomic DNA. Translation: CAI20950.1.
BC005122 mRNA. Translation: AAH05122.1.
AL137598 mRNA. Translation: CAB70834.1.
AK002083 mRNA. Translation: BAA92076.1. Different initiation.
AK022768 mRNA. Translation: BAB14236.1. Different initiation.

IPI

IPI00299263.

PIR

T46305.

RefSeq

NP_001135765.1. NM_001142293.1.
NP_055385.3. NM_014570.4.

UniGene

Hs.685225.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CRW	NMR	-	A	1-136	[»]

ProteinModelPortal

Q9NP61.

SMR

Q9NP61. Positions 3-136.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NP61. 3 interactions.

STRING

Q9NP61.

PTM databases

PhosphoSite

Q9NP61.

Polymorphism databases

DMDM

21263420.

Proteomic databases

PeptideAtlas

Q9NP61.

PRIDE

Q9NP61.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263245; ENSP00000263245; ENSG00000242247.

GeneID

26286.

KEGG

hsa:26286.

UCSC

uc003bdd.1. human.

Organism-specific databases

CTD

26286.

GeneCards

GC22M043192.

H-InvDB

HIX0016547.

HGNC

HGNC:661. ARFGAP3.

HPA

HPA000638.

MIM

612439. gene.

neXtProt

NX_Q9NP61.

PharmGKB

PA35024.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16306.

GeneTree

ENSGT00390000005436.

HOVERGEN

HBG050563.

InParanoid

Q9NP61.

OrthoDB

EOG4N8R4S.

PhylomeDB

Q9NP61.

Gene expression databases

ArrayExpress

Q9NP61.

Bgee

Q9NP61.

CleanEx

HS_ARFGAP1.
HS_ARFGAP3.

Genevestigator

Q9NP61.

GermOnline

ENSG00000100262. Homo sapiens.

Family and domain databases

InterPro

IPR001164. ArfGAP.
[Graphical view]

KO

K12493.

Pfam

PF01412. ArfGap. 1 hit.
[Graphical view]

PRINTS

PR00405. REVINTRACTNG.

SMART

SM00105. ArfGap. 1 hit.
[Graphical view]

SUPFAM

SSF57863. ArfGAP. 1 hit.

PROSITE

PS50115. ARFGAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

48617.

SOURCE

Search...

Entry information

Entry name

ARFG3_HUMAN

Accession

Primary (citable) accession number: Q9NP61
Secondary accession number(s): Q9BSC6 , Q9H9J0, Q9NT10, Q9NUP5, Q9Y4V3, Q9Y4V4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 27, 2002
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 110 of the entry and version 1 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.