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Q9Y6D5

- BIG2_HUMAN

UniProt

Q9Y6D5 - BIG2_HUMAN

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Protein

Brefeldin A-inhibited guanine nucleotide-exchange protein 2

Gene

ARFGEF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.7 Publications

Enzyme regulationi

Inhibited by brefeldin A.

GO - Molecular functioni

  1. ARF guanyl-nucleotide exchange factor activity Source: UniProtKB
  2. GABA receptor binding Source: UniProtKB
  3. guanyl-nucleotide exchange factor activity Source: MGI
  4. protein kinase A regulatory subunit binding Source: UniProtKB

GO - Biological processi

  1. endomembrane system organization Source: UniProtKB
  2. endosome organization Source: UniProtKB
  3. exocytosis Source: ProtInc
  4. Golgi to plasma membrane transport Source: UniProtKB
  5. intracellular signal transduction Source: MGI
  6. positive regulation of GTPase activity Source: GOC
  7. positive regulation of tumor necrosis factor production Source: UniProtKB
  8. protein transport Source: UniProtKB-KW
  9. receptor recycling Source: UniProtKB
  10. regulation of ARF protein signal transduction Source: InterPro
  11. vesicle-mediated transport Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ARFGEF2
Synonyms:ARFGEP2, BIG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:15853. ARFGEF2.

Subcellular locationi

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.

GO - Cellular componenti

  1. asymmetric synapse Source: UniProtKB
  2. axonemal microtubule Source: UniProtKB
  3. cell junction Source: UniProtKB-KW
  4. cytoplasmic vesicle Source: UniProtKB
  5. cytosol Source: MGI
  6. dendritic spine Source: UniProtKB
  7. Golgi membrane Source: UniProtKB
  8. membrane Source: UniProtKB
  9. microtubule organizing center Source: UniProtKB
  10. recycling endosome Source: UniProtKB
  11. symmetric synapse Source: UniProtKB
  12. trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endosome, Golgi apparatus, Membrane, Synapse

Pathology & Biotechi

Involvement in diseasei

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 PVNH2.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti209 – 2091E → K in PVNH2. 1 Publication
Corresponds to variant rs28937880 [ dbSNP | Ensembl ].
VAR_037438

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi289 – 2891V → W: Abolishes interaction with PRKAR2B and impairs TNFRSF1A release. 1 Publication
Mutagenesisi534 – 5341V → W: Abolishes interaction with PRKAR2B and impairs TNFRSF1A release. 1 Publication
Mutagenesisi738 – 7381E → K: Disturbs membrane organization at the TGN, impairs association of the AP-1 complex and GGA1 with the TGN membranes. 2 Publications

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi608097. phenotype.
Orphaneti98892. Periventricular nodular heterotopia.
PharmGKBiPA24945.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17851785Brefeldin A-inhibited guanine nucleotide-exchange protein 2PRO_0000120208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei218 – 2181Phosphoserine4 Publications
Modified residuei227 – 2271Phosphoserine5 Publications
Modified residuei277 – 2771Phosphoserine1 Publication
Modified residuei614 – 6141Phosphoserine1 Publication
Modified residuei616 – 6161PhosphothreonineBy similarity
Modified residuei1525 – 15251Phosphoserine2 Publications
Modified residuei1528 – 15281Phosphoserine5 Publications
Modified residuei1782 – 17821Phosphoserine1 Publication

Post-translational modificationi

In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1.8 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y6D5.
PaxDbiQ9Y6D5.
PRIDEiQ9Y6D5.

PTM databases

PhosphoSiteiQ9Y6D5.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9Y6D5.
CleanExiHS_ARFGEF2.
ExpressionAtlasiQ9Y6D5. baseline and differential.
GenevestigatoriQ9Y6D5.

Organism-specific databases

HPAiCAB026382.
HPA026078.

Interactioni

Subunit structurei

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).By similarityCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
ARFGEF1Q9Y6D63EBI-2837511,EBI-1044254
EXOC7Q9UPT5-14EBI-2837511,EBI-6251402
MYCBPQ994175EBI-2837511,EBI-716185

Protein-protein interaction databases

BioGridi115815. 28 interactions.
DIPiDIP-48794N.
IntActiQ9Y6D5. 12 interactions.
MINTiMINT-1200143.
STRINGi9606.ENSP00000360985.

Structurei

Secondary structure

1
1785
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi641 – 6433
Turni644 – 6485
Helixi649 – 6546
Helixi658 – 66710
Turni674 – 6785
Helixi679 – 6824
Helixi690 – 6945
Turni695 – 6984
Turni702 – 7054
Helixi706 – 7127
Helixi723 – 7297
Helixi739 – 75315
Helixi766 – 77712
Turni778 – 7825
Turni796 – 7983
Beta strandi799 – 8013
Beta strandi804 – 8085
Helixi812 – 82211

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L8NX-ray2.86A635-836[»]
3SWVX-ray3.00A635-836[»]
ProteinModelPortaliQ9Y6D5.
SMRiQ9Y6D5. Positions 637-828.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini654 – 785132SEC7PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 224223DCB; DCB:DCB domain and DCB:HUS domain interactionAdd
BLAST
Regioni508 – 52821HUS; DCB:HUS domain interactionAdd
BLAST

Sequence similaritiesi

Contains 1 SEC7 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5307.
GeneTreeiENSGT00760000119036.
HOGENOMiHOG000181045.
HOVERGENiHBG004846.
InParanoidiQ9Y6D5.
KOiK18442.
OMAiDALAYFI.
OrthoDBiEOG7QVM1S.
PhylomeDBiQ9Y6D5.
TreeFamiTF300714.

Family and domain databases

Gene3Di1.10.1000.11. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR015403. DUF1981_Sec7_assoc.
IPR023394. Sec7_alpha_orthog.
IPR000904. Sec7_dom.
[Graphical view]
PfamiPF09324. DUF1981. 1 hit.
PF01369. Sec7. 1 hit.
[Graphical view]
SMARTiSM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF48425. SSF48425. 1 hit.
PROSITEiPS50190. SEC7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y6D5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQESQTKSMF VSRALEKILA DKEVKRPQHS QLRRACQVAL DEIKAEIEKQ
60 70 80 90 100
RLGTAAPPKA NFIEADKYFL PFELACQSKS PRVVSTSLDC LQKLIAYGHI
110 120 130 140 150
TGNAPDSGAP GKRLIDRIVE TICSCFQGPQ TDEGVQLQII KALLTAVTSP
160 170 180 190 200
HIEIHEGTIL QTVRTCYNIY LASKNLINQT TAKATLTQML NVIFTRMENQ
210 220 230 240 250
VLQEARELEK PIQSKPQSPV IQAAAVSPKF VRLKHSQAQS KPTTPEKTDL
260 270 280 290 300
TNGEHARSDS GKVSTENGDA PRERGSSLSG TDDGAQEVVK DILEDVVTSA
310 320 330 340 350
IKEAAEKHGL TEPERVLGEL ECQECAIPPG VDENSQTNGI ADDRQSLSSA
360 370 380 390 400
DNLESDAQGH QVAARFSHVL QKDAFLVFRS LCKLSMKPLG EGPPDPKSHE
410 420 430 440 450
LRSKVVSLQL LLSVLQNAGP VFRTHEMFIN AIKQYLCVAL SKNGVSSVPD
460 470 480 490 500
VFELSLAIFL TLLSNFKMHL KMQIEVFFKE IFLNILETST SSFEHRWMVI
510 520 530 540 550
QTLTRICADA QCVVDIYVNY DCDLNAANIF ERLVNDLSKI AQGRSGHELG
560 570 580 590 600
MTPLQELSLR KKGLECLVSI LKCMVEWSKD LYVNPNHQTS LGQERLTDQE
610 620 630 640 650
IGDGKGLDMA RRCSVTSMES TVSSGTQTTV QDDPEQFEVI KQQKEIIEHG
660 670 680 690 700
IELFNKKPKR GIQFLQEQGM LGTSVEDIAQ FLHQEERLDS TQVGDFLGDS
710 720 730 740 750
ARFNKEVMYA YVDQLDFCEK EFVSALRTFL EGFRLPGEAQ KIDRLMEKFA
760 770 780 790 800
ARYIECNQGQ TLFASADTAY VLAYSIIMLT TDLHSPQVKN KMTKEQYIKM
810 820 830 840 850
NRGINDSKDL PEEYLSSIYE EIEGKKIAMK ETKELTIATK STKQNVASEK
860 870 880 890 900
QRRLLYNLEM EQMAKTAKAL MEAVSHAKAP FTSATHLDHV RPMFKLVWTP
910 920 930 940 950
LLAAYSIGLQ NCDDTEVASL CLEGIRCAIR IACIFGMQLE RDAYVQALAR
960 970 980 990 1000
FSLLTASSSI TEMKQKNIDT IKTLITVAHT DGNYLGNSWH EILKCISQLE
1010 1020 1030 1040 1050
LAQLIGTGVK TRYLSGSGRE REGSLKGHTL AGEEFMGLGL GNLVSGGVDK
1060 1070 1080 1090 1100
RQMASFQESV GETSSQSVVV AVDRIFTGST RLDGNAIVDF VRWLCAVSMD
1110 1120 1130 1140 1150
ELASPHHPRM FSLQKIVEIS YYNMNRIRLQ WSRIWHVIGD HFNKVGCNPN
1160 1170 1180 1190 1200
EDVAIFAVDS LRQLSMKFLE KGELANFRFQ KDFLRPFEHI MKKNRSPTIR
1210 1220 1230 1240 1250
DMAIRCIAQM VNSQAANIRS GWKNIFAVFH QAASDHDGNI VELAFQTTCH
1260 1270 1280 1290 1300
IVTTIFQHHF PAAIDSFQDA VKCLSEFACN AAFPDTSMEA IRLIRFCGKY
1310 1320 1330 1340 1350
VSERPRVLQE YTSDDMNVAP GDRVWVRGWF PILFELSCII NRCKLDVRTR
1360 1370 1380 1390 1400
GLTVMFEIMK SYGHTFEKHW WQDLFRIVFR IFDNMKLPEQ LSEKSEWMTT
1410 1420 1430 1440 1450
TCNHALYAIC DVFTQFYEAL NEVLLSDVFA QLQWCVKQDN EQLARSGTNC
1460 1470 1480 1490 1500
LENLVISNGE KFSPEVWDET CNCMLDIFKT TIPHVLLTWR PVGMEEDSSE
1510 1520 1530 1540 1550
KHLDVDLDRQ SLSSIDKNPS ERGQSQLSNP TDDSWKGRPY ANQKLFASLL
1560 1570 1580 1590 1600
IKCVVQLELI QTIDNIVFYP ATSKKEDAEH MVAAQQDTLD ADIHIETEDQ
1610 1620 1630 1640 1650
GMYKYMSSQH LFKLLDCLQE SHSFSKAFNS NYEQRTVLWR AGFKGKSKPN
1660 1670 1680 1690 1700
LLKQETSSLA CCLRILFRMY VDENRRDSWE EIQQRLLTVC SEALAYFITV
1710 1720 1730 1740 1750
NSESHREAWT SLLLLLLTKT LKINDEKFKA HASMYYPYLC EIMQFDLIPE
1760 1770 1780
LRAVLRKFFL RIGVVYKIWI PEEPSQVPAA LSPVW
Length:1,785
Mass (Da):202,038
Last modified:March 6, 2007 - v3
Checksum:iD419106E5BAF19C2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071E → R in AAD38428. (PubMed:10212200)Curated
Sequence conflicti962 – 9621E → K in AAD38428. (PubMed:10212200)Curated
Sequence conflicti1049 – 10491D → N in AAD38428. (PubMed:10212200)Curated
Sequence conflicti1763 – 17631G → S in AAD38428. (PubMed:10212200)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti209 – 2091E → K in PVNH2. 1 Publication
Corresponds to variant rs28937880 [ dbSNP | Ensembl ].
VAR_037438
Natural varianti527 – 5271A → V.
Corresponds to variant rs6063343 [ dbSNP | Ensembl ].
VAR_028750
Natural varianti794 – 7941K → E in a breast cancer sample; somatic mutation. 1 Publication
VAR_036156
Natural varianti802 – 8021R → Q.1 Publication
VAR_069404

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF084521 mRNA. Translation: AAD38428.1.
AL049537, AL121903 Genomic DNA. Translation: CAI19320.1.
AL121903, AL049537 Genomic DNA. Translation: CAI19614.1.
CCDSiCCDS13411.1.
RefSeqiNP_006411.2. NM_006420.2.
UniGeneiHs.62578.

Genome annotation databases

EnsembliENST00000371917; ENSP00000360985; ENSG00000124198.
GeneIDi10564.
KEGGihsa:10564.
UCSCiuc002xtx.4. human.

Polymorphism databases

DMDMi146329988.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF084521 mRNA. Translation: AAD38428.1 .
AL049537 , AL121903 Genomic DNA. Translation: CAI19320.1 .
AL121903 , AL049537 Genomic DNA. Translation: CAI19614.1 .
CCDSi CCDS13411.1.
RefSeqi NP_006411.2. NM_006420.2.
UniGenei Hs.62578.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3L8N X-ray 2.86 A 635-836 [» ]
3SWV X-ray 3.00 A 635-836 [» ]
ProteinModelPortali Q9Y6D5.
SMRi Q9Y6D5. Positions 637-828.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115815. 28 interactions.
DIPi DIP-48794N.
IntActi Q9Y6D5. 12 interactions.
MINTi MINT-1200143.
STRINGi 9606.ENSP00000360985.

PTM databases

PhosphoSitei Q9Y6D5.

Polymorphism databases

DMDMi 146329988.

Proteomic databases

MaxQBi Q9Y6D5.
PaxDbi Q9Y6D5.
PRIDEi Q9Y6D5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371917 ; ENSP00000360985 ; ENSG00000124198 .
GeneIDi 10564.
KEGGi hsa:10564.
UCSCi uc002xtx.4. human.

Organism-specific databases

CTDi 10564.
GeneCardsi GC20P047538.
H-InvDB HIX0015895.
HGNCi HGNC:15853. ARFGEF2.
HPAi CAB026382.
HPA026078.
MIMi 605371. gene.
608097. phenotype.
neXtProti NX_Q9Y6D5.
Orphaneti 98892. Periventricular nodular heterotopia.
PharmGKBi PA24945.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5307.
GeneTreei ENSGT00760000119036.
HOGENOMi HOG000181045.
HOVERGENi HBG004846.
InParanoidi Q9Y6D5.
KOi K18442.
OMAi DALAYFI.
OrthoDBi EOG7QVM1S.
PhylomeDBi Q9Y6D5.
TreeFami TF300714.

Enzyme and pathway databases

Reactomei REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

Miscellaneous databases

ChiTaRSi ARFGEF2. human.
GeneWikii ARFGEF2.
GenomeRNAii 10564.
NextBioi 40093.
PROi Q9Y6D5.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y6D5.
CleanExi HS_ARFGEF2.
ExpressionAtlasi Q9Y6D5. baseline and differential.
Genevestigatori Q9Y6D5.

Family and domain databases

Gene3Di 1.10.1000.11. 1 hit.
InterProi IPR016024. ARM-type_fold.
IPR015403. DUF1981_Sec7_assoc.
IPR023394. Sec7_alpha_orthog.
IPR000904. Sec7_dom.
[Graphical view ]
Pfami PF09324. DUF1981. 1 hit.
PF01369. Sec7. 1 hit.
[Graphical view ]
SMARTi SM00222. Sec7. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 3 hits.
SSF48425. SSF48425. 1 hit.
PROSITEi PS50190. SEC7. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-794.
  28. Cited for: VARIANT GLN-802.

Entry informationi

Entry nameiBIG2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6D5
Secondary accession number(s): Q5TFT9, Q9NTS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: March 6, 2007
Last modified: October 29, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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