Q8N6H7 (ARFG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Name:	ARFGAP2
Synonyms:	ZNF289
ORF Names:	Nbla10535

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	521 AA.
Sequence status	Complete.
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 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.

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 Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of GTPase activity Inferred from electronic annotation. Source: GOC protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of ARF GTPase activity Inferred from electronic annotation. Source: InterPro vesicle-mediated transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: HPA
Molecular_function	ARF GTPase activator activity Inferred from electronic annotation. Source: InterPro 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 – 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.9 Ref.10 Ref.11 Ref.13

Modified residue

337

1

Phosphoserine By similarity

Modified residue

368

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11

Modified residue

432

1

Phosphoserine Ref.9 Ref.11 Ref.13

Modified residue

433

1

Phosphoserine Ref.13

Natural variations

Natural variant

143

1

P → R.
Corresponds to variant rs11542793 [ dbSNP | Ensembl ].

VAR_048321

Natural variant

339

1

R → H.
Corresponds to variant rs34662994 [ dbSNP | Ensembl ].

VAR_048322

Natural variant

406

1

R → W.
Corresponds to variant rs35950498 [ dbSNP | Ensembl ].

VAR_048323

Natural variant

411

1

S → N. Ref.5
Corresponds to variant rs3740691 [ dbSNP | Ensembl ].

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

1

.

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.

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.

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.

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.

.

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.

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.

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521

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	Q8N6H7 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 16655EBA94D29E81	FASTA	521	56,720
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[14]	"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.

IPI

IPI00297322.

RefSeq

NP_001229761.1. NM_001242832.1.
NP_115765.2. NM_032389.4.

UniGene

Hs.436204.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2P57	X-ray	1.80	A	3-130	[»]

ProteinModelPortal

Q8N6H7.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000327309.

PTM databases

PhosphoSite

Q8N6H7.

Polymorphism databases

DMDM

74729129.

Proteomic databases

PaxDb

Q8N6H7.

PeptideAtlas

Q8N6H7.

PRIDE

Q8N6H7.

Protocols and materials databases

DNASU

84364.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000524782; ENSP00000434442; ENSG00000149182.

GeneID

84364.

KEGG

hsa:84364.

UCSC

uc001ndt.3. human.

Organism-specific databases

CTD

84364.

GeneCards

GC11M047185.

HGNC

HGNC:13504. ARFGAP2.

HPA

HPA016649.
HPA018152.

MIM

606908. gene.

neXtProt

NX_Q8N6H7.

PharmGKB

PA162376868.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5347.

HOGENOM

HOG000162970.

HOVERGEN

HBG050563.

InParanoid

Q8N6H7.

KO

K12493.

OMA

FASRWDT.

OrthoDB

EOG447FTM.

PhylomeDB

Q8N6H7.

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

EvolutionaryTrace

Q8N6H7.

GenomeRNAi

84364.

NextBio

74137.

SOURCE

Search...

Entry information

Entry name

ARFG2_HUMAN

Accession

Primary (citable) accession number: Q8N6H7
Secondary accession number(s): D3DQQ9 , Q3LIF2, Q8N3I1, Q96SX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 20, 2007
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 94 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.