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Reviewed, UniProtKB/Swiss-Prot Q8N6H7 (ARFG2_HUMAN)

Last modified November 24, 2009. Version 60. 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 2
      Short name=ARF GAP 2
Alternative name(s):
    GTPase-activating protein ZNF289
    Zinc finger protein 289
Gene names
Name: ARFGAP2
Synonyms: ZNF289
ORF Names: Nbla10535
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length521 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). Implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. Ref.7

Subunit structure

Interacts with the coatomer complex. Interacts with the C-terminal appendage domain of COPG. Ref.7 Ref.5

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.7

Miscellaneous

Vero cells overexpressing truncated ARFGAP2 show accumulation of cholera toxin A subunit in the Golgi complex rather than the endoplasmic reticulum.

Sequence similarities

Contains 1 Arf-GAP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521ADP-ribosylation factor GTPase-activating protein 2
PRO_0000278468

Regions

Domain11 – 127117Arf-GAP
Zinc finger26 – 4924C4-type
Region97 – 521425Required for interaction with coatomer
Coiled coil242 – 30867 Potential

Amino acid modifications

Modified residue1461Phosphoserine Ref.6 Ref.8 Ref.9
Modified residue3371Phosphoserine By similarity
Modified residue3681Phosphoserine Ref.8 Ref.9
Modified residue4321Phosphoserine Ref.9
Modified residue4981Phosphoserine Ref.6

Natural variations

Natural variant1431P → R: dbSNP rs11542793.
VAR_048321
Natural variant3391R → H: dbSNP rs34662994.
VAR_048322
Natural variant4061R → W: dbSNP rs35950498.
VAR_048323
Natural variant4111S → N: dbSNP rs3740691. Ref.4
VAR_030780

Experimental info

Sequence conflict401T → M in BAB55144. Ref.1
Sequence conflict1071N → S in BAB55144. Ref.1

Secondary structure

......................... 521
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8N6H7-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 16655EBA94D29E81

FASTA52156,720
        10         20         30         40         50         60 
MAAEPNKTEI QTLFKRLRAV PTNKACFDCG AKNPSWASIT YGVFLCIDCS GVHRSLGVHL 

        70         80         90        100        110        120 
SFIRSTELDS NWNWFQLRCM QVGGNANATA FFRQHGCTAN DANTKYNSRA AQMYREKIRQ 

       130        140        150        160        170        180 
LGSAALARHG TDLWIDNMSS AVPNHSPEKK DSDFFTEHTQ PPAWDAPATE PSGTQQPAPS 

       190        200        210        220        230        240 
TESSGLAQPE HGPNTDLLGT SPKASLELKS SIIGKKKPAA AKKGLGAKKG LGAQKVSSQS 

       250        260        270        280        290        300 
FSEIERQAQV AEKLREQQAA DAKKQAEESM VASMRLAYQE LQIDRKKEEK KLQNLEGKKR 

       310        320        330        340        350        360 
EQAERLGMGL VSRSSVSHSV LSEMQVIEQE TPVSAKSSRS QLDLFDDVGT FASGPPKYKD 

       370        380        390        400        410        420 
NPFSLGESFG SRWDTDAAWG MDRVEEKEPE VTISSIRPIS ERATNRREVE SRSSGLESSE 

       430        440        450        460        470        480 
ARQKFAGAKA ISSDMFFGRE VDAEYEARSR LQQLSGSSAI SSSDLFGDMD GAHGAGSVSL 

       490        500        510        520 
GNVLPTADIA QFKQGVKSVA GKMAVLANGV MNSLQDRYGS Y 

« Hide

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].
Tissue: Teratocarcinoma.
[2]"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].
Tissue: Eye.
[3]"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 4-521.
Tissue: Amygdala.
[4]"Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
Cancer Lett. 197:63-68(2003) [PubMed: 12880961] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-521, VARIANT ASN-411.
Tissue: Neuroblastoma.
[5]"Gamma-COP appendage domain -- structure and function."
Watson P.J., Frigerio G., Collins B.M., Duden R., Owen D.J.
Traffic 5:79-88(2004) [PubMed: 14690497] [Abstract]
Cited for: INTERACTION WITH COPG.
[6]"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-146 AND SER-498, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COATOMER.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 AND SER-368, MASS SPECTROMETRY.
[9]"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-146; SER-368 AND SER-432, MASS SPECTROMETRY.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]"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-432, MASS SPECTROMETRY.
[12]"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-146; SER-368 AND SER-432, MASS SPECTROMETRY.
Tissue: T-cell.
[13]"Gap domain of ZNF289, an ID1-regulated zinc finger protein."
Structural genomics consortium (SGC)
Submitted (MAR-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-130.

Cross-references

Sequence databases

AK027482 mRNA. Translation: BAB55144.1.
BC030148 mRNA. Translation: AAH30148.1.
AL834337 mRNA. Translation: CAD39004.1.
AB073358 mRNA. Translation: BAE45716.1.
IPIIPI00297322.
RefSeqNP_115765.2.
UniGeneHs.436204

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2P57X-ray1.80A3-130[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8N6H7.

PTM databases

PhosphoSiteQ8N6H7.

Proteomic databases

PeptideAtlasQ8N6H7.
PRIDEQ8N6H7.

Genome annotation databases

EnsemblENST00000319543; ENSP00000327309; ENSG00000149182; Homo sapiens. [Genome view]
GeneID84364.
KEGGhsa:84364.
UCSCuc001ndt.1. human.

Organism-specific databases

CTD84364.
GeneCardsGC11M047143.
HGNCHGNC:13504. ARFGAP2.
HPAHPA016649.
HPA018152.
MIM606908. gene.
PharmGKBPA37790.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ8N6H7.
OMAWDAPATE
OrthoDBEOG9R7XWC

Gene expression databases

ArrayExpressQ8N6H7.
BgeeQ8N6H7.
CleanExHS_ARFGAP2.
GenevestigatorQ8N6H7.

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

NextBio74137.
SOURCESearch...

Entry information

Entry nameARFG2_HUMAN
AccessionPrimary (citable) accession number: Q8N6H7
Secondary accession number(s): Q3LIF2, Q8N3I1, Q96SX7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: October 1, 2002
Last modified: November 24, 2009
This is version 60 of the entry and version 1 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.

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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