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Q8N6H7 (ARFG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 COPG1. Ref.6 Ref.7

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

Initiator methionine11Removed Ref.14
Chain2 – 521520ADP-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 residue21N-acetylalanine Ref.14
Modified residue1461Phosphoserine Ref.9 Ref.10 Ref.11 Ref.13
Modified residue2401Phosphoserine By similarity
Modified residue3681Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11
Modified residue4321Phosphoserine Ref.9 Ref.11 Ref.13
Modified residue4331Phosphoserine Ref.13

Natural variations

Natural variant1431P → R.
Corresponds to variant rs11542793 [ dbSNP | Ensembl ].
VAR_048321
Natural variant3391R → H.
Corresponds to variant rs34662994 [ dbSNP | Ensembl ].
VAR_048322
Natural variant4061R → W.
Corresponds to variant rs35950498 [ dbSNP | Ensembl ].
VAR_048323
Natural variant4111S → N. Ref.5
Corresponds to variant rs3740691 [ dbSNP | Ensembl ].
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 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Teratocarcinoma.
[2]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].
[3]"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].
Tissue: Eye.
[4]"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 4-521.
Tissue: Amygdala.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-521, VARIANT ASN-411.
Tissue: Neuroblastoma.
[6]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COPG1.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-368 AND SER-432, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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 SER-146 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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 SER-146; SER-368 AND SER-432, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-432 AND SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK027482 mRNA. Translation: BAB55144.1.
CH471064 Genomic DNA. Translation: EAW67963.1.
CH471064 Genomic DNA. Translation: EAW67968.1.
BC030148 mRNA. Translation: AAH30148.1.
AL834337 mRNA. Translation: CAD39004.1.
AB073358 mRNA. Translation: BAE45716.1.
RefSeqNP_001229761.1. NM_001242832.1.
NP_115765.2. NM_032389.4.
UniGeneHs.436204.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P57X-ray1.80A3-130[»]
ProteinModelPortalQ8N6H7.
SMRQ8N6H7. Positions 4-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124065. 3 interactions.
STRING9606.ENSP00000327309.

PTM databases

PhosphoSiteQ8N6H7.

Polymorphism databases

DMDM74729129.

Proteomic databases

PaxDbQ8N6H7.
PeptideAtlasQ8N6H7.
PRIDEQ8N6H7.

Protocols and materials databases

DNASU84364.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000524782; ENSP00000434442; ENSG00000149182.
GeneID84364.
KEGGhsa:84364.
UCSCuc001ndt.3. human.

Organism-specific databases

CTD84364.
GeneCardsGC11M047185.
HGNCHGNC:13504. ARFGAP2.
HPAHPA016649.
HPA018152.
MIM606908. gene.
neXtProtNX_Q8N6H7.
PharmGKBPA162376868.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5347.
HOGENOMHOG000162970.
HOVERGENHBG050563.
InParanoidQ8N6H7.
KOK12493.
OMADTDATWG.
OrthoDBEOG7B8S42.
PhylomeDBQ8N6H7.
TreeFamTF313985.

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

EvolutionaryTraceQ8N6H7.
GenomeRNAi84364.
NextBio74137.
PROQ8N6H7.
SOURCESearch...

Entry information

Entry nameARFG2_HUMAN
AccessionPrimary (citable) accession number: Q8N6H7
Secondary accession number(s): D3DQQ9 expand/collapse secondary AC list , Q3LIF2, Q8N3I1, Q96SX7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM