Reviewed,
UniProtKB/Swiss-Prot Q8N6H7 (ARFG2_HUMAN)
Last modified
November 24, 2009.
Version 60.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
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| Organism | Homo sapiens (Human) [Complete proteome] | ||||||
| Taxonomic identifier | 9606 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 521 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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. |
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 | Phosphoprotein |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of ARF GTPase activityInferred from electronic annotation. Source: InterPro vesicle-mediated transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | Golgi apparatus Inferred from direct assay. Source: HPA plasma membraneInferred from direct assay. Source: HPA |
| Molecular function | ARF GTPase activator activity Inferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 521 | 521 | ADP-ribosylation factor GTPase-activating protein 2 | PRO_0000278468 | |||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||
| Domain | 11 – 127 | 117 | Arf-GAP | ||||||||||||||||||||||||||||||
| Zinc finger | 26 – 49 | 24 | C4-type | ||||||||||||||||||||||||||||||
| Region | 97 – 521 | 425 | Required for interaction with coatomer | ||||||||||||||||||||||||||||||
| Coiled coil | 242 – 308 | 67 | Potential | ||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||
| Modified residue | 146 | 1 | Phosphoserine Ref.6 Ref.8 Ref.9 | ||||||||||||||||||||||||||||||
| Modified residue | 337 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||
| Modified residue | 368 | 1 | Phosphoserine Ref.8 Ref.9 | ||||||||||||||||||||||||||||||
| Modified residue | 432 | 1 | Phosphoserine Ref.9 | ||||||||||||||||||||||||||||||
| Modified residue | 498 | 1 | Phosphoserine Ref.6 | ||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||
| Natural variant | 143 | 1 | P → R: dbSNP rs11542793. | VAR_048321 | |||||||||||||||||||||||||||||
| Natural variant | 339 | 1 | R → H: dbSNP rs34662994. | VAR_048322 | |||||||||||||||||||||||||||||
| Natural variant | 406 | 1 | R → W: dbSNP rs35950498. | VAR_048323 | |||||||||||||||||||||||||||||
| Natural variant | 411 | 1 | S → N: dbSNP rs3740691. Ref.4 | VAR_030780 | |||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||
| Sequence conflict | 40 | 1 | T → M in BAB55144. Ref.1 | ||||||||||||||||||||||||||||||
| Sequence conflict | 107 | 1 | N → S in BAB55144. Ref.1 | ||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||
| Helix | 7 – 19 | 13 | |||||||||||||||||||||||||||||||
| Helix | 21 – 24 | 4 | |||||||||||||||||||||||||||||||
| Turn | 27 – 29 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 36 – 38 | 3 | |||||||||||||||||||||||||||||||
| Turn | 39 – 42 | 4 | |||||||||||||||||||||||||||||||
| Beta strand | 43 – 45 | 3 | |||||||||||||||||||||||||||||||
| Helix | 47 – 56 | 10 | |||||||||||||||||||||||||||||||
| Turn | 58 – 60 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 63 – 68 | 6 | |||||||||||||||||||||||||||||||
| Helix | 74 – 82 | 9 | |||||||||||||||||||||||||||||||
| Helix | 85 – 94 | 10 | |||||||||||||||||||||||||||||||
| Helix | 102 – 106 | 5 | |||||||||||||||||||||||||||||||
| Helix | 109 – 124 | 16 | |||||||||||||||||||||||||||||||
Sequences
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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. 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. | |||||||||||||
| IPI | IPI00297322. | ||||||||||||
| RefSeq | NP_115765.2. | ||||||||||||
| UniGene | Hs.436204 | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | Q8N6H7. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q8N6H7. | ||||||||||||
Proteomic databases | |||||||||||||
| PeptideAtlas | Q8N6H7. | ||||||||||||
| PRIDE | Q8N6H7. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000319543; ENSP00000327309; ENSG00000149182; Homo sapiens. [Genome view] | ||||||||||||
| GeneID | 84364. | ||||||||||||
| KEGG | hsa:84364. | ||||||||||||
| UCSC | uc001ndt.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 84364. | ||||||||||||
| GeneCards | GC11M047143. | ||||||||||||
| HGNC | HGNC:13504. ARFGAP2. | ||||||||||||
| HPA | HPA016649. HPA018152. | ||||||||||||
| MIM | 606908. gene. | ||||||||||||
| PharmGKB | PA37790. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | Q8N6H7. | ||||||||||||
| OMA | WDAPATE | ||||||||||||
| OrthoDB | EOG9R7XWC | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q8N6H7. | ||||||||||||
| Bgee | Q8N6H7. | ||||||||||||
| CleanEx | HS_ARFGAP2. | ||||||||||||
| Genevestigator | Q8N6H7. | ||||||||||||
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 Resources | |||||||||||||
| NextBio | 74137. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | ARFG2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q8N6H7 Secondary accession number(s): Q3LIF2, Q8N3I1, Q96SX7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| 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. | ||||||||
Relevant documents
| Human chromosome 11 Human chromosome 11: 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 |

Clusters with


