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Q9Y6D5 (BIG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Brefeldin A-inhibited guanine nucleotide-exchange protein 2

Short name=Brefeldin A-inhibited GEP 2
Alternative name(s):
ADP-ribosylation factor guanine nucleotide-exchange factor 2
Gene names
Name:ARFGEF2
Synonyms:ARFGEP2, BIG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1785 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extend on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Ref.4 Ref.5 Ref.6 Ref.10 Ref.11 Ref.14 Ref.21

Enzyme regulation

Inhibited by brefeldin A.

Subunit structure

Homodimer Probable. Interacts with BIG1; both proteins are probably part of the same or very similar macromolecular complexes. Interacts with PRKAR1A, PRKAR2A, PRKAR1B, PRKAR2B, PPP1CC, PDE3A, TNFRSF1A, MYCBP and EXOC7. Interacts with GABRB1, GABRB2 and GABRB3 By similarity. Ref.3 Ref.5 Ref.7 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.19

Subcellular location

Cytoplasm. Membrane. Golgi apparatus. Cytoplasmperinuclear region. Golgi apparatustrans-Golgi network By similarity. Endosome By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cell projectiondendrite By similarity. Cytoplasmic vesicle By similarity. Cell junctionsynapse By similarity. Cytoplasmcytoskeleton By similarity. Note: Translocates from cytoplasm to membranes upon cAMP treatment. Localized in recycling endosomes. Ref.3 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10

Tissue specificity

Expressed in placenta, lung, heart, brain, kidney and pancreas.

Post-translational modification

In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1. Ref.13

Involvement in disease

Periventricular nodular heterotopia 2 (PVNH2) [MIM:608097]: A developmental disorder characterized by the presence of periventricular nodules of cerebral gray matter, resulting from a failure of neurons to migrate normally from the lateral ventricular proliferative zone, where they are formed, to the cerebral cortex. PVNH2 is an autosomal recessive form characterized by microcephaly (small brain), severe developmental delay and recurrent infections. No anomalies extrinsic to the central nervous system, such as dysmorphic features or grossly abnormal endocrine or other conditions, are associated with PVNH2.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26

Sequence similarities

Contains 1 SEC7 domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell junction
Cell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Endosome
Golgi apparatus
Membrane
Synapse
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   Molecular functionGuanine-nucleotide releasing factor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to plasma membrane transport

Inferred from mutant phenotype Ref.11. Source: UniProtKB

endomembrane system organization

Inferred from mutant phenotype Ref.21. Source: UniProtKB

endosome organization

Inferred from mutant phenotype Ref.21. Source: UniProtKB

exocytosis

Traceable author statement Ref.1. Source: ProtInc

intracellular signal transduction

Inferred from direct assay Ref.5. Source: MGI

positive regulation of tumor necrosis factor production

Inferred from mutant phenotype Ref.11. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

receptor recycling

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of ARF protein signal transduction

Inferred from electronic annotation. Source: InterPro

regulation of GTPase activity

Inferred from direct assay Ref.1Ref.6. Source: GOC

vesicle-mediated transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentGolgi membrane

Inferred from direct assay Ref.3. Source: UniProtKB

asymmetric synapse

Inferred from sequence or structural similarity. Source: UniProtKB

axonemal microtubule

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay Ref.5. Source: MGI

dendritic spine

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from direct assay Ref.5. Source: MGI

microtubule organizing center

Inferred from direct assay Ref.7. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

recycling endosome

Inferred from direct assay Ref.6. Source: UniProtKB

symmetric synapse

Inferred from sequence or structural similarity. Source: UniProtKB

trans-Golgi network

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionARF guanyl-nucleotide exchange factor activity

Inferred from direct assay Ref.6. Source: UniProtKB

GABA receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

guanyl-nucleotide exchange factor activity

Inferred from direct assay Ref.1. Source: MGI

protein kinase A regulatory subunit binding

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17851785Brefeldin A-inhibited guanine nucleotide-exchange protein 2
PRO_0000120208

Regions

Domain654 – 785132SEC7
Region2 – 224223DCB; DCB:DCB domain and DCB:HUS domain interaction
Region508 – 52821HUS; DCB:HUS domain interaction

Amino acid modifications

Modified residue11N-acetylmethionine Ref.25
Modified residue2181Phosphoserine Ref.8 Ref.15 Ref.22 Ref.24
Modified residue2271Phosphoserine Ref.8 Ref.15 Ref.20 Ref.22 Ref.24
Modified residue2771Phosphoserine Ref.20
Modified residue6141Phosphoserine Ref.16
Modified residue6161Phosphothreonine By similarity
Modified residue15251Phosphoserine Ref.8 Ref.20
Modified residue15281Phosphoserine Ref.8 Ref.15 Ref.18 Ref.20 Ref.22
Modified residue17821Phosphoserine Ref.15

Natural variations

Natural variant2091E → K in PVNH2. Ref.26
Corresponds to variant rs28937880 [ dbSNP | Ensembl ].
VAR_037438
Natural variant5271A → V.
Corresponds to variant rs6063343 [ dbSNP | Ensembl ].
VAR_028750
Natural variant7941K → E in a breast cancer sample; somatic mutation. Ref.27
VAR_036156
Natural variant8021R → Q. Ref.28
VAR_069404

Experimental info

Mutagenesis2891V → W: Abolishes interaction with PRKAR2B and impairs TNFRSF1A release. Ref.14
Mutagenesis5341V → W: Abolishes interaction with PRKAR2B and impairs TNFRSF1A release. Ref.14
Mutagenesis7381E → K: Disturbs membrane organization at the TGN, impairs association of the AP-1 complex and GGA1 with the TGN membranes. Ref.4 Ref.6
Sequence conflict2071E → R in AAD38428. Ref.1
Sequence conflict9621E → K in AAD38428. Ref.1
Sequence conflict10491D → N in AAD38428. Ref.1
Sequence conflict17631G → S in AAD38428. Ref.1

Secondary structure

.............................. 1785
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y6D5 [UniParc].

Last modified March 6, 2007. Version 3.
Checksum: D419106E5BAF19C2

FASTA1,785202,038
        10         20         30         40         50         60 
MQESQTKSMF VSRALEKILA DKEVKRPQHS QLRRACQVAL DEIKAEIEKQ RLGTAAPPKA 

        70         80         90        100        110        120 
NFIEADKYFL PFELACQSKS PRVVSTSLDC LQKLIAYGHI TGNAPDSGAP GKRLIDRIVE 

       130        140        150        160        170        180 
TICSCFQGPQ TDEGVQLQII KALLTAVTSP HIEIHEGTIL QTVRTCYNIY LASKNLINQT 

       190        200        210        220        230        240 
TAKATLTQML NVIFTRMENQ VLQEARELEK PIQSKPQSPV IQAAAVSPKF VRLKHSQAQS 

       250        260        270        280        290        300 
KPTTPEKTDL TNGEHARSDS GKVSTENGDA PRERGSSLSG TDDGAQEVVK DILEDVVTSA 

       310        320        330        340        350        360 
IKEAAEKHGL TEPERVLGEL ECQECAIPPG VDENSQTNGI ADDRQSLSSA DNLESDAQGH 

       370        380        390        400        410        420 
QVAARFSHVL QKDAFLVFRS LCKLSMKPLG EGPPDPKSHE LRSKVVSLQL LLSVLQNAGP 

       430        440        450        460        470        480 
VFRTHEMFIN AIKQYLCVAL SKNGVSSVPD VFELSLAIFL TLLSNFKMHL KMQIEVFFKE 

       490        500        510        520        530        540 
IFLNILETST SSFEHRWMVI QTLTRICADA QCVVDIYVNY DCDLNAANIF ERLVNDLSKI 

       550        560        570        580        590        600 
AQGRSGHELG MTPLQELSLR KKGLECLVSI LKCMVEWSKD LYVNPNHQTS LGQERLTDQE 

       610        620        630        640        650        660 
IGDGKGLDMA RRCSVTSMES TVSSGTQTTV QDDPEQFEVI KQQKEIIEHG IELFNKKPKR 

       670        680        690        700        710        720 
GIQFLQEQGM LGTSVEDIAQ FLHQEERLDS TQVGDFLGDS ARFNKEVMYA YVDQLDFCEK 

       730        740        750        760        770        780 
EFVSALRTFL EGFRLPGEAQ KIDRLMEKFA ARYIECNQGQ TLFASADTAY VLAYSIIMLT 

       790        800        810        820        830        840 
TDLHSPQVKN KMTKEQYIKM NRGINDSKDL PEEYLSSIYE EIEGKKIAMK ETKELTIATK 

       850        860        870        880        890        900 
STKQNVASEK QRRLLYNLEM EQMAKTAKAL MEAVSHAKAP FTSATHLDHV RPMFKLVWTP 

       910        920        930        940        950        960 
LLAAYSIGLQ NCDDTEVASL CLEGIRCAIR IACIFGMQLE RDAYVQALAR FSLLTASSSI 

       970        980        990       1000       1010       1020 
TEMKQKNIDT IKTLITVAHT DGNYLGNSWH EILKCISQLE LAQLIGTGVK TRYLSGSGRE 

      1030       1040       1050       1060       1070       1080 
REGSLKGHTL AGEEFMGLGL GNLVSGGVDK RQMASFQESV GETSSQSVVV AVDRIFTGST 

      1090       1100       1110       1120       1130       1140 
RLDGNAIVDF VRWLCAVSMD ELASPHHPRM FSLQKIVEIS YYNMNRIRLQ WSRIWHVIGD 

      1150       1160       1170       1180       1190       1200 
HFNKVGCNPN EDVAIFAVDS LRQLSMKFLE KGELANFRFQ KDFLRPFEHI MKKNRSPTIR 

      1210       1220       1230       1240       1250       1260 
DMAIRCIAQM VNSQAANIRS GWKNIFAVFH QAASDHDGNI VELAFQTTCH IVTTIFQHHF 

      1270       1280       1290       1300       1310       1320 
PAAIDSFQDA VKCLSEFACN AAFPDTSMEA IRLIRFCGKY VSERPRVLQE YTSDDMNVAP 

      1330       1340       1350       1360       1370       1380 
GDRVWVRGWF PILFELSCII NRCKLDVRTR GLTVMFEIMK SYGHTFEKHW WQDLFRIVFR 

      1390       1400       1410       1420       1430       1440 
IFDNMKLPEQ LSEKSEWMTT TCNHALYAIC DVFTQFYEAL NEVLLSDVFA QLQWCVKQDN 

      1450       1460       1470       1480       1490       1500 
EQLARSGTNC LENLVISNGE KFSPEVWDET CNCMLDIFKT TIPHVLLTWR PVGMEEDSSE 

      1510       1520       1530       1540       1550       1560 
KHLDVDLDRQ SLSSIDKNPS ERGQSQLSNP TDDSWKGRPY ANQKLFASLL IKCVVQLELI 

      1570       1580       1590       1600       1610       1620 
QTIDNIVFYP ATSKKEDAEH MVAAQQDTLD ADIHIETEDQ GMYKYMSSQH LFKLLDCLQE 

      1630       1640       1650       1660       1670       1680 
SHSFSKAFNS NYEQRTVLWR AGFKGKSKPN LLKQETSSLA CCLRILFRMY VDENRRDSWE 

      1690       1700       1710       1720       1730       1740 
EIQQRLLTVC SEALAYFITV NSESHREAWT SLLLLLLTKT LKINDEKFKA HASMYYPYLC 

      1750       1760       1770       1780 
EIMQFDLIPE LRAVLRKFFL RIGVVYKIWI PEEPSQVPAA LSPVW 

« Hide

References

« Hide 'large scale' references
[1]"Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors."
Togawa A., Morinaga N., Ogasawara M., Moss J., Vaughan M.
J. Biol. Chem. 274:12308-12315(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Identification and localization of two brefeldin A-inhibited guanine nucleotide-exchange proteins for ADP-ribosylation factors in a macromolecular complex."
Yamaji R., Adamik R., Takeda K., Togawa A., Pacheco-Rodriguez G., Ferrans V.J., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 97:2567-2572(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BIG1.
[4]"Dominant-negative mutant of BIG2, an ARF-guanine nucleotide exchange factor, specifically affects membrane trafficking from the trans-Golgi network through inhibiting membrane association of AP-1 and GGA coat proteins."
Shinotsuka C., Waguri S., Wakasugi M., Uchiyama Y., Nakayama K.
Biochem. Biophys. Res. Commun. 294:254-260(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLU-738.
[5]"Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2)."
Li H., Adamik R., Pacheco-Rodriguez G., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 100:1627-1632(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRKAR1A; PRKAR2A; PRKAR1B AND PRKAR2B, SUBCELLULAR LOCATION.
[6]"BIG2, a guanine nucleotide exchange factor for ADP-ribosylation factors: its localization to recycling endosomes and implication in the endosome integrity."
Shin H.W., Morinaga N., Noda M., Nakayama K.
Mol. Biol. Cell 15:5283-5294(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-738.
[7]"Interaction of BIG2, a brefeldin A-inhibited guanine nucleotide-exchange protein, with exocyst protein Exo70."
Xu K.F., Shen X., Li H., Pacheco-Rodriguez G., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 102:2784-2789(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EXOC7, SUBCELLULAR LOCATION.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-227; SER-1525 AND SER-1528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"AMY-1 (associate of Myc-1) localization to the trans-Golgi network through interacting with BIG2, a guanine-nucleotide exchange factor for ADP-ribosylation factors."
Ishizaki R., Shin H.W., Iguchi-Ariga S.M., Ariga H., Nakayama K.
Genes Cells 11:949-959(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MYCBP.
[10]"Association of brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2) with recycling endosomes during transferrin uptake."
Shen X., Xu K.F., Fan Q., Pacheco-Rodriguez G., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 103:2635-2640(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"The brefeldin A-inhibited guanine nucleotide-exchange protein, BIG2, regulates the constitutive release of TNFR1 exosome-like vesicles."
Islam A., Shen X., Hiroi T., Moss J., Vaughan M., Levine S.J.
J. Biol. Chem. 282:9591-9599(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TNFRSF1A.
[12]"Interactions between conserved domains within homodimers in the BIG1, BIG2, and GBF1 Arf guanine nucleotide exchange factors."
Ramaen O., Joubert A., Simister P., Belgareh-Touze N., Olivares-Sanchez M.C., Zeeh J.C., Chantalat S., Golinelli-Cohen M.P., Jackson C.L., Biou V., Cherfils J.
J. Biol. Chem. 282:28834-28842(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[13]"Regulation of brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) and BIG2 activity via PKA and protein phosphatase 1gamma."
Kuroda F., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 104:3201-3206(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH PPP1CC.
[14]"cAMP-dependent protein kinase A (PKA) signaling induces TNFR1 exosome-like vesicle release via anchoring of PKA regulatory subunit RIIbeta to BIG2."
Islam A., Jones H., Hiroi T., Lam J., Zhang J., Moss J., Vaughan M., Levine S.J.
J. Biol. Chem. 283:25364-25371(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRKAR2B, MUTAGENESIS OF VAL-289 AND VAL-534.
[15]"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-218; SER-227; SER-1528 AND SER-1782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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-614, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Interaction of phosphodiesterase 3A with brefeldin A-inhibited guanine nucleotide-exchange proteins BIG1 and BIG2 and effect on ARF1 activity."
Puxeddu E., Uhart M., Li C.C., Ahmad F., Pacheco-Rodriguez G., Manganiello V.C., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 106:6158-6163(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDE3A.
[20]"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-227; SER-277; SER-1525 AND SER-1528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"Specific functions of BIG1 and BIG2 in endomembrane organization."
Boal F., Stephens D.J.
PLoS ONE 5:E9898-E9898(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"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-218; SER-227 AND SER-1528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"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].
[24]"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-218 AND SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Mutations in ARFGEF2 implicate vesicle trafficking in neural progenitor proliferation and migration in the human cerebral cortex."
Sheen V.L., Ganesh V.S., Topcu M., Sebire G., Bodell A., Hill R.S., Grant P.E., Shugart Y.Y., Imitola J., Khoury S.J., Guerrini R., Walsh C.A.
Nat. Genet. 36:69-76(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PVNH2 LYS-209.
[27]"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] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-794.
[28]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-802.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF084521 mRNA. Translation: AAD38428.1.
AL049537, AL121903 Genomic DNA. Translation: CAI19320.1.
AL121903, AL049537 Genomic DNA. Translation: CAI19614.1.
RefSeqNP_006411.2. NM_006420.2.
UniGeneHs.62578.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3L8NX-ray2.86A635-836[»]
3SWVX-ray3.00A635-836[»]
ProteinModelPortalQ9Y6D5.
SMRQ9Y6D5. Positions 637-828.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115815. 17 interactions.
DIPDIP-48794N.
IntActQ9Y6D5. 12 interactions.
MINTMINT-1200143.
STRING9606.ENSP00000360985.

PTM databases

PhosphoSiteQ9Y6D5.

Polymorphism databases

DMDM146329988.

Proteomic databases

PaxDbQ9Y6D5.
PRIDEQ9Y6D5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371917; ENSP00000360985; ENSG00000124198.
GeneID10564.
KEGGhsa:10564.
UCSCuc002xtx.4. human.

Organism-specific databases

CTD10564.
GeneCardsGC20P047538.
H-InvDBHIX0015895.
HGNCHGNC:15853. ARFGEF2.
HPACAB026382.
HPA026078.
MIM605371. gene.
608097. phenotype.
neXtProtNX_Q9Y6D5.
Orphanet98892. Periventricular nodular heterotopia.
PharmGKBPA24945.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5307.
HOGENOMHOG000181045.
HOVERGENHBG004846.
InParanoidQ9Y6D5.
OMAEVWDETC.
OrthoDBEOG7QVM1S.
PhylomeDBQ9Y6D5.
TreeFamTF300714.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9Y6D5.
BgeeQ9Y6D5.
CleanExHS_ARFGEF2.
GenevestigatorQ9Y6D5.

Family and domain databases

Gene3D1.10.1000.11. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR015403. DUF1981_Sec7_assoc.
IPR023394. Sec7_alpha_orthog.
IPR000904. Sec7_dom.
[Graphical view]
PfamPF09324. DUF1981. 1 hit.
PF01369. Sec7. 1 hit.
[Graphical view]
SMARTSM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
SSF48425. SSF48425. 1 hit.
PROSITEPS50190. SEC7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARFGEF2. human.
GeneWikiARFGEF2.
GenomeRNAi10564.
NextBio40093.
PROQ9Y6D5.
SOURCESearch...

Entry information

Entry nameBIG2_HUMAN
AccessionPrimary (citable) accession number: Q9Y6D5
Secondary accession number(s): Q5TFT9, Q9NTS1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: March 6, 2007
Last modified: April 16, 2014
This is version 124 of the entry and version 3 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 20

Human chromosome 20: entries, gene names and cross-references to MIM