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Q9Y6D6 (BIG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. 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 1

Short name=Brefeldin A-inhibited GEP 1
Alternative name(s):
ADP-ribosylation factor guanine nucleotide-exchange factor 1
p200 ARF guanine nucleotide exchange factor
p200 ARF-GEP1
Gene names
Name:ARFGEF1
Synonyms:ARFGEP1, BIG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1849 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competetive RhoA binding. The function in the nucleus remains to be determined. Ref.6 Ref.9 Ref.13 Ref.24 Ref.25

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 FKBP2, DPY30, MYO9B, PRKAR1A, PRKAR2A, PPP1CC and PDE3A. Interacts with KANK1; however, colocalization cannot be experimentally confirmed. Interacts with NCL, FBL, NUP62 and U3 small nucleolar RNA. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.14 Ref.17 Ref.19 Ref.20 Ref.24

Subcellular location

Cytoplasm. Cytoplasmperinuclear region. Golgi apparatus. Golgi apparatustrans-Golgi network By similarity. Nucleus. Nucleusnucleolus. Nucleus matrix. Membrane. Note: Translocates from cytoplasm to membranes and nucleus upon cAMP treatment. Ref.5 Ref.6 Ref.8 Ref.11 Ref.24

Tissue specificity

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

Post-translational modification

Phosphorylated. In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1. Ref.14

Sequence similarities

Contains 1 SEC7 domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionGuanine-nucleotide releasing factor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi organization

Inferred from mutant phenotype Ref.13Ref.25. Source: UniProtKB

endomembrane system organization

Inferred from mutant phenotype Ref.25. Source: UniProtKB

exocytosis

Traceable author statement Ref.1. Source: ProtInc

negative regulation of Rho GTPase activity

Inferred from direct assay Ref.9. Source: UniProtKB

negative regulation of actin filament polymerization

Inferred from mutant phenotype Ref.24. Source: UniProtKB

positive regulation of protein glycosylation in Golgi

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of wound healing

Inferred from mutant phenotype Ref.24. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of ARF protein signal transduction

Inferred from electronic annotation. Source: InterPro

regulation of establishment of cell polarity

Inferred from mutant phenotype Ref.24. Source: UniProtKB

vesicle-mediated transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

Golgi membrane

Inferred from direct assay Ref.5. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay Ref.5. Source: UniProtKB

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay Ref.8. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from direct assay Ref.24. Source: UniProtKB

small nuclear ribonucleoprotein complex

Inferred from direct assay Ref.17. Source: UniProtKB

trans-Golgi network

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionARF guanyl-nucleotide exchange factor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

guanyl-nucleotide exchange factor activity

Inferred from direct assay Ref.9. Source: UniProtKB

myosin binding

Inferred from physical interaction Ref.9. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16417406Ref.19. Source: UniProtKB

protein kinase A regulatory subunit binding

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18491849Brefeldin A-inhibited guanine nucleotide-exchange protein 1
PRO_0000120207

Regions

Domain709 – 840132SEC7
Region2 – 224223DCB; DCB:DCB domain and DCB:HUS domain interaction
Region557 – 57721HUS; DCB:HUS domain interaction
Motif711 – 7155Nuclear localization signal (NLS)

Amino acid modifications

Modified residue10791Phosphoserine Ref.26
Modified residue15691Phosphoserine Ref.10 Ref.15 Ref.16 Ref.22 Ref.26

Natural variations

Natural variant2731D → Y.
Corresponds to variant rs4321984 [ dbSNP | Ensembl ].
VAR_028749
Natural variant3161G → E in a colorectal cancer sample; somatic mutation. Ref.27
VAR_036155

Experimental info

Mutagenesis2211E → K: No effect on self-association. Ref.12
Mutagenesis712 – 7143KPK → AAA: Inhibits nuclear localization. Ref.11
Mutagenesis8831S → A: Abolishes cAMP-induced nuclear localization. Ref.11
Mutagenesis8831S → D: No effect on cAMP-induced nuclear localization. Ref.11
Sequence conflict2331Q → P in AAD38427. Ref.1
Sequence conflict6201L → S in AAD38427. Ref.1
Sequence conflict10551E → K in AAD38427. Ref.1
Sequence conflict15901V → A in BAA91912. Ref.3

Secondary structure

....................... 1849
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y6D6 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 1EB2547F28F63BCA

FASTA1,849208,767
        10         20         30         40         50         60 
MYEGKKTKNM FLTRALEKIL ADKEVKKAHH SQLRKACEVA LEEIKAETEK QSPPHGEAKA 

        70         80         90        100        110        120 
GSSTLPPVKS KTNFIEADKY FLPFELACQS KCPRIVSTSL DCLQKLIAYG HLTGNAPDST 

       130        140        150        160        170        180 
TPGKKLIDRI IETICGCFQG PQTDEGVQLQ IIKALLTAVT SQHIEIHEGT VLQAVRTCYN 

       190        200        210        220        230        240 
IYLASKNLIN QTTAKATLTQ MLNVIFARME NQALQEAKQM EKERHRQHHH LLQSPVSHHE 

       250        260        270        280        290        300 
PESPQLRYLP PQTVDHISQE HEGDLDLHTN DVDKSLQDDT EPENGSDISS AENEQTEADQ 

       310        320        330        340        350        360 
ATAAETLSKN EVLYDGENHD CEEKPQDIVQ NIVEEMVNIV VGDMGEGTTI NASADGNIGT 

       370        380        390        400        410        420 
IEDGSDSENI QANGIPGTPI SVAYTPSLPD DRLSVSSNDT QESGNSSGPS PGAKFSHILQ 

       430        440        450        460        470        480 
KDAFLVFRSL CKLSMKPLSD GPPDPKSHEL RSKILSLQLL LSILQNAGPI FRTNEMFINA 

       490        500        510        520        530        540 
IKQYLCVALS KNGVSSVPEV FELSLSIFLT LLSNFKTHLK MQIEVFFKEI FLYILETSTS 

       550        560        570        580        590        600 
SFDHKWMVIQ TLTRICADAQ SVVDIYVNYD CDLNAANIFE RLVNDLSKIA QGRGSQELGM 

       610        620        630        640        650        660 
SNVQELSLRK KGLECLVSIL KCMVEWSKDQ YVNPNSQTTL GQEKPSEQEM SEIKHPETIN 

       670        680        690        700        710        720 
RYGSLNSLES TSSSGIGSYS TQMSGTDNPE QFEVLKQQKE IIEQGIDLFN KKPKRGIQYL 

       730        740        750        760        770        780 
QEQGMLGTTP EDIAQFLHQE ERLDSTQVGE FLGDNDKFNK EVMYAYVDQH DFSGKDFVSA 

       790        800        810        820        830        840 
LRMFLEGFRL PGEAQKIDRL MEKFAARYLE CNQGQTLFAS ADTAYVLAYS IIMLTTDLHS 

       850        860        870        880        890        900 
PQVKNKMTKE QYIKMNRGIN DSKDLPEEYL SAIYNEIAGK KISMKETKEL TIPTKSSKQN 

       910        920        930        940        950        960 
VASEKQRRLL YNLEMEQMAK TAKALMEAVS HVQAPFTSAT HLEHVRPMFK LAWTPFLAAF 

       970        980        990       1000       1010       1020 
SVGLQDCDDT EVASLCLEGI RCAIRIACIF SIQLERDAYV QALARFTLLT VSSGITEMKQ 

      1030       1040       1050       1060       1070       1080 
KNIDTIKTLI TVAHTDGNYL GNSWHEILKC ISQLELAQLI GTGVKPRYIS GTVRGREGSL 

      1090       1100       1110       1120       1130       1140 
TGTKDQAPDE FVGLGLVGGN VDWKQIASIQ ESIGETSSQS VVVAVDRIFT GSTRLDGNAI 

      1150       1160       1170       1180       1190       1200 
VDFVRWLCAV SMDELLSTTH PRMFSLQKIV EISYYNMGRI RLQWSRIWEV IGDHFNKVGC 

      1210       1220       1230       1240       1250       1260 
NPNEDVAIFA VDSLRQLSMK FLEKGELANF RFQKDFLRPF EHIMKRNRSP TIRDMVVRCI 

      1270       1280       1290       1300       1310       1320 
AQMVNSQAAN IRSGWKNIFS VFHLAASDQD ESIVELAFQT TGHIVTLVFE KHFPATIDSF 

      1330       1340       1350       1360       1370       1380 
QDAVKCLSEF ACNAAFPDTS MEAIRLIRHC AKYVSDRPQA FKEYTSDDMN VAPEDRVWVR 

      1390       1400       1410       1420       1430       1440 
GWFPILFELS CIINRCKLDV RTRGLTVMFE IMKTYGHTYE KHWWQDLFRI VFRIFDNMKL 

      1450       1460       1470       1480       1490       1500 
PEQQTEKAEW MTTTCNHALY AICDVFTQYL EVLSDVLLDD IFAQLYWCVQ QDNEQLARSG 

      1510       1520       1530       1540       1550       1560 
TNCLENVVIL NGEKFTLEIW DKTCNCTLDI FKTTIPHALL TWRPNSGETA PPPPSPVSEK 

      1570       1580       1590       1600       1610       1620 
PLDTISQKSV DIHDSIQPRS VDNRPQAPLV SASAVNEEVS KIKSTAKFPE QKLFAALLIK 

      1630       1640       1650       1660       1670       1680 
CVVQLELIQT IDNIVFFPAT SKKEDAENLA AAQRDAVDFD VRVDTQDQGM YRFLTSQQLF 

      1690       1700       1710       1720       1730       1740 
KLLDCLLESH RFAKAFNSNN EQRTALWKAG FKGKSKPNLL KQETSSLACG LRILFRMYMD 

      1750       1760       1770       1780       1790       1800 
ESRVSAWEEV QQRLLNVCSE ALSYFLTLTS ESHREAWTNL LLLFLTKVLK ISDNRFKAHA 

      1810       1820       1830       1840 
SFYYPLLCEI MQFDLIPELR AVLRRFFLRI GVVFQISQPP EQELGINKQ 

« 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]"p200 ARF-GEP1: a Golgi-localized guanine nucleotide exchange protein whose Sec7 domain is targeted by the drug brefeldin A."
Mansour S.J., Skaug J., Zhao X.-H., Giordano J., Scherer S.W., Melancon P.
Proc. Natl. Acad. Sci. U.S.A. 96:7968-7973(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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] OF 1341-1849.
Tissue: Ovarian carcinoma.
[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 1637-1849.
Tissue: Testis.
[5]"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 BIG2.
[6]"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 AND PRKAR2A, SUBCELLULAR LOCATION.
[7]"Interaction of FK506-binding protein 13 with brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1): effects of FK506."
Padilla P.I., Chang M.J., Pacheco-Rodriguez G., Adamik R., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 100:2322-2327(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FKBP2.
[8]"Nuclear localization and molecular partners of BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors."
Padilla P.I., Pacheco-Rodriguez G., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 101:2752-2757(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NCL AND NUP62.
[9]"BIG1 is a binding partner of myosin IXb and regulates its Rho-GTPase activating protein activity."
Saeki N., Tokuo H., Ikebe M.
J. Biol. Chem. 280:10128-10134(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYO9B.
[10]"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-1569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Effect of protein kinase A on accumulation of brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) in HepG2 cell nuclei."
Citterio C., Jones H.D., Pacheco-Rodriguez G., Islam A., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 103:2683-2688(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 712-LYS--LYS-714 AND SER-883.
[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, MUTAGENESIS OF GLU-221.
[13]"BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is required for correct glycosylation and function of integrin beta1."
Shen X., Hong M.S., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 104:1230-1235(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"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.
[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-1569, 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-1569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Association of guanine nucleotide-exchange protein BIG1 in HepG2 cell nuclei with nucleolin, U3 snoRNA, and fibrillarin."
Padilla P.I., Uhart M., Pacheco-Rodriguez G., Peculis B.A., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 105:3357-3361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCL; FBL; NUP62 AND U3 SMALL NUCLEOLAR RNA, IDENTIFICATION IN SMALL NUCLEAR RIBONUCLEOPROTEIN COMPLEX.
[18]"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].
[19]"A role of histone H3 lysine 4 methyltransferase components in endosomal trafficking."
Xu Z., Gong Q., Xia B., Groves B., Zimmermann M., Mugler C., Mu D., Matsumoto B., Seaman M., Ma D.
J. Cell Biol. 186:343-353(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DPY30.
[20]"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.
[21]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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-1569, 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]"Effects of brefeldin A-inhibited guanine nucleotide-exchange (BIG) 1 and KANK1 proteins on cell polarity and directed migration during wound healing."
Li C.C., Kuo J.C., Waterman C.M., Kiyama R., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 108:19228-19233(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KANK1.
[25]"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.
[26]"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-1079 AND SER-1569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-316.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF084520 mRNA. Translation: AAD38427.1.
AF111162 mRNA. Translation: AAD43651.1.
AK001788 mRNA. Translation: BAA91912.1.
AL117446 mRNA. Translation: CAB55931.1.
CCDSCCDS6199.1.
PIRT17241.
RefSeqNP_006412.2. NM_006421.4.
XP_005251191.1. XM_005251134.2.
UniGeneHs.656902.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LTLX-ray2.20A/B691-889[»]
ProteinModelPortalQ9Y6D6.
SMRQ9Y6D6. Positions 695-885.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115816. 12 interactions.
DIPDIP-29748N.
IntActQ9Y6D6. 10 interactions.
MINTMINT-1728435.
STRING9606.ENSP00000262215.

PTM databases

PhosphoSiteQ9Y6D6.

Polymorphism databases

DMDM116241267.

Proteomic databases

MaxQBQ9Y6D6.
PaxDbQ9Y6D6.
PeptideAtlasQ9Y6D6.
PRIDEQ9Y6D6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262215; ENSP00000262215; ENSG00000066777.
GeneID10565.
KEGGhsa:10565.
UCSCuc003xxo.2. human.

Organism-specific databases

CTD10565.
GeneCardsGC08M068085.
HGNCHGNC:15772. ARFGEF1.
HPAHPA023399.
HPA023822.
MIM604141. gene.
neXtProtNX_Q9Y6D6.
PharmGKBPA134908197.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5307.
HOGENOMHOG000181045.
HOVERGENHBG004846.
InParanoidQ9Y6D6.
OMAILLMPCH.
PhylomeDBQ9Y6D6.
TreeFamTF300714.

Gene expression databases

ArrayExpressQ9Y6D6.
BgeeQ9Y6D6.
CleanExHS_ARFGEF1.
GenevestigatorQ9Y6D6.

Family and domain databases

Gene3D1.10.1000.11. 1 hit.
1.25.10.10. 4 hits.
InterProIPR011989. ARM-like.
IPR016024. 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

ChiTaRSARFGEF1. human.
EvolutionaryTraceQ9Y6D6.
GeneWikiARFGEF1.
GenomeRNAi10565.
NextBio40097.
PROQ9Y6D6.
SOURCESearch...

Entry information

Entry nameBIG1_HUMAN
AccessionPrimary (citable) accession number: Q9Y6D6
Secondary accession number(s): Q9NV46, Q9UFV2, Q9UNL0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 127 of the entry and version 2 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 8

Human chromosome 8: entries, gene names and cross-references to MIM