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Reviewed, UniProtKB/Swiss-Prot Q9NP61 (ARFG3_HUMAN)

Last modified June 16, 2009. Version 83. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ADP-ribosylation factor GTPase-activating protein 3
      Short name=ARF GAP 3
Gene names
Name: ARFGAP3
Synonyms: ARFGAP1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length516 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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, pituary 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 516516ADP-ribosylation factor GTPase-activating protein 3
PRO_0000074193

Regions

Domain10 – 126117Arf-GAP
Zinc finger25 – 4824C4-type
Coiled coil243 – 26321 Potential
Compositional bias348 – 37730Ser-rich

Amino acid modifications

Modified residue1431Phosphoserine Ref.9
Modified residue2701Phosphoserine Ref.12
Modified residue3311Phosphoserine Ref.10 Ref.13
Modified residue4531Phosphoserine Ref.13

Natural variations

Natural variant2311S → G: dbSNP rs9607957.
VAR_055523
Natural variant2901E → G in a breast cancer sample; somatic mutation. Ref.16
VAR_036177
Natural variant3551S → R: dbSNP rs1018448. Ref.3 Ref.5 Ref.7
VAR_013447
Natural variant3701S → G: dbSNP rs16986123.
VAR_055524
Natural variant4681Q → H: dbSNP rs35498349.
VAR_055525
Natural variant4821A → T: dbSNP rs36003980.
VAR_055526
Natural variant4901Q → R: dbSNP rs11551619.
VAR_055527

Experimental info

Sequence conflict3391K → R in BAA92076. Ref.7
Sequence conflict4011T → A in BAA92076. Ref.7
Sequence conflict4581S → P in BAB14236. Ref.7

Secondary structure

......................... 516
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NP61-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: E355E56A5D867F8E

FASTA51656,928
        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 

« Hide

References

« Hide '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:RESEARCH84.1-RESEARCH84.11(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. expand/collapse author list , 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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder 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. 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] 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: Epithelium.
[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: Epithelium.
[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.
[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.
[14]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]"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.
[16]"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. expand/collapse author list , 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

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.
IPIIPI00299263.
PIRT46305.
RefSeqNP_001135765.1.
NP_055385.3.
UniGeneHs.685225

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2CRWNMR-A1-136[»]
ModBaseSearch...

PTM databases

PhosphoSiteQ9NP61.

Proteomic databases

PeptideAtlasQ9NP61.
PRIDEQ9NP61.

Genome annotation databases

EnsemblENSG00000100262. Homo sapiens. [Contig view]
GeneID26286.
KEGGhsa:26286.

Organism-specific databases

GeneCardsGC22M041517.
H-InvDBHIX0009609.
HIX0016547.
HGNCHGNC:661. ARFGAP3.
HPAHPA000638.
MIM612439. gene.
PharmGKBPA35024.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9NP61.
OMAQ9NP61. KPDYEPV.

Gene expression databases

ArrayExpressQ9NP61.
BgeeQ9NP61.
CleanExHS_ARFGAP1.
HS_ARFGAP3.
GermOnlineENSG00000100262. 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

NextBio48617.
SOURCESearch...

Entry information

Entry nameARFG3_HUMAN
AccessionPrimary (citable) accession number: Q9NP61
Secondary accession number(s): Q9BSC6 expand/collapse secondary AC list , Q9H9J0, Q9NT10, Q9NUP5, Q9Y4V3, Q9Y4V4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 22

Human chromosome 22: 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents