Q9Y6D6 (BIG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	1849 AA.
Sequence status	Complete.
Protein existence	Evidence 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.23 Ref.24
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.18 Ref.19 Ref.23
Subcellular location	Cytoplasm. Cytoplasm › perinuclear region. Golgi apparatus. Golgi apparatus › trans-Golgi network By similarity. Nucleus. Nucleus › nucleolus. Nucleus matrix. Membrane. Note: Translocates from cytoplasm to membranes and nucleus upon cAMP treatment. Ref.5 Ref.6 Ref.8 Ref.11 Ref.23
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 process	Protein transport Transport
Cellular component	Cytoplasm Golgi apparatus Membrane Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Golgi organization Inferred from mutant phenotype Ref.13Ref.24. Source: UniProtKB endomembrane system organization Inferred from mutant phenotype Ref.24. 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.23. 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.23. 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.23. Source: UniProtKB
Cellular_component	Golgi membrane Inferred from direct assay Ref.5. Source: UniProtKB 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 perinuclear region of cytoplasm Inferred from direct assay Ref.23. 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_function	ARF guanyl-nucleotide exchange factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome protein kinase A regulatory subunit binding Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARFGEF2	Q9Y6D5	3	EBI-1044254,EBI-2837511
KIF21A	Q7Z4S6	3	EBI-1044254,EBI-2691397
KIF21A	Q7Z4S6-2	4	EBI-1044254,EBI-6251716
MYCBP	Q99417	3	EBI-1044254,EBI-716185
MYO9B	Q13459-2	2	EBI-1044254,EBI-6251250

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1849

1849

Brefeldin A-inhibited guanine nucleotide-exchange protein 1

PRO_0000120207

Regions

Domain

709 – 840

132

SEC7

Region

2 – 224

223

DCB; DCB:DCB domain and DCB:HUS domain interaction

Region

557 – 577

21

HUS; DCB:HUS domain interaction

Motif

711 – 715

5

Nuclear localization signal (NLS)

Amino acid modifications

Modified residue

1079

1

Phosphoserine Ref.25

Modified residue

1569

1

Phosphoserine Ref.10 Ref.15 Ref.16 Ref.21 Ref.25

Natural variations

Natural variant

273

1

D → Y.
Corresponds to variant rs4321984 [ dbSNP | Ensembl ].

VAR_028749

Natural variant

316

1

G → E in a colorectal cancer sample; somatic mutation. Ref.26

VAR_036155

Experimental info

Mutagenesis

221

1

E → K: No effect on self-association. Ref.12

Mutagenesis

712 – 714

3

KPK → AAA: Inhibits nuclear localization. Ref.11

Mutagenesis

883

1

S → A: Abolishes cAMP-induced nuclear localization. Ref.11

Mutagenesis

883

1

S → D: No effect on cAMP-induced nuclear localization. Ref.11

Sequence conflict

233

1

Q → P in AAD38427. Ref.1

Sequence conflict

620

1

L → S in AAD38427. Ref.1

Sequence conflict

1055

1

E → K in AAD38427. Ref.1

Sequence conflict

1590

1

V → A in BAA91912. Ref.3

Secondary structure

1

.

.

.

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.

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.

.

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.

.

.

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1849

Helix Strand Turn

Details...

Helix

698 – 711

14

Helix

713 – 722

10

Helix

730 – 739

10

Helix

745 – 752

8

Helix

757 – 768

12

Helix

777 – 786

10

Helix

794 – 810

17

Helix

821 – 838

18

Helix

849 – 855

7

Beta strand

861 – 864

4

Helix

867 – 879

13

Sequences

	Sequence		Length	Mass (Da)
	Q9Y6D6 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 1EB2547F28F63BCA	FASTA	1,849	208,767
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[21]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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].
[23]	"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.
[24]	"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.
[25]	"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, MASS SPECTROMETRY.
[26]	"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. , 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.

IPI

IPI00002188.

PIR

T17241.

RefSeq

NP_006412.2. NM_006421.4.

UniGene

Hs.656902.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LTL	X-ray	2.20	A/B	691-889	[»]

ProteinModelPortal

Q9Y6D6.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29748N.

IntAct

Q9Y6D6. 10 interactions.

STRING

9606.ENSP00000262215.

PTM databases

PhosphoSite

Q9Y6D6.

Polymorphism databases

DMDM

116241267.

Proteomic databases

PaxDb

Q9Y6D6.

PeptideAtlas

Q9Y6D6.

PRIDE

Q9Y6D6.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000262215; ENSP00000262215; ENSG00000066777.

GeneID

10565.

KEGG

hsa:10565.

UCSC

uc003xxo.2. human.

Organism-specific databases

CTD

10565.

GeneCards

GC08M068085.

HGNC

HGNC:15772. ARFGEF1.

HPA

HPA023399.
HPA023822.

MIM

604141. gene.

neXtProt

NX_Q9Y6D6.

PharmGKB

PA134908197.

GenAtlas

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Phylogenomic databases

eggNOG

COG5307.

HOGENOM

HOG000181045.

HOVERGEN

HBG004846.

InParanoid

Q9Y6D6.

OMA

DPHTNDV.

OrthoDB

EOG4V9TPR.

PhylomeDB

Q9Y6D6.

Gene expression databases

ArrayExpress

Q9Y6D6.

Bgee

Q9Y6D6.

CleanEx

HS_ARFGEF1.

Genevestigator

Q9Y6D6.

GermOnline

ENSG00000066777. Homo sapiens.

Family and domain databases

Gene3D

1.10.1000.11. 1 hit.
1.25.10.10. 4 hits.

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR015403. DUF1981_SEC7_assoc.
IPR000904. Sec7.
IPR023394. SEC7_alpha_orthog.
[Graphical view]

Pfam

PF09324. DUF1981. 1 hit.
PF01369. Sec7. 1 hit.
[Graphical view]

SMART

SM00222. Sec7. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.
SSF48425. Sec7. 1 hit.

PROSITE

PS50190. SEC7. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

ARFGEF1. human.

EvolutionaryTrace

Q9Y6D6.

GenomeRNAi

10565.

NextBio

40097.

SOURCE

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Entry information

Entry name

BIG1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 115 of the entry and version 2 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.