CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023987
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Brefeldin A-inhibited guanine nucleotide-exchange protein 1 
Protein Synonyms/Alias
 Brefeldin A-inhibited GEP 1; ADP-ribosylation factor guanine nucleotide-exchange factor 1; p200 ARF guanine nucleotide exchange factor; p200 ARF-GEP1 
Gene Name
 ARFGEF1 
Gene Synonyms/Alias
 ARFGEP1; BIG1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1224LSMKFLEKGELANFRubiquitination[1]
1694LESHRFAKAFNSNNEubiquitination[2, 3]
1708EQRTALWKAGFKGKSacetylation[4]
1708EQRTALWKAGFKGKSubiquitination[3]
Reference
 [1] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 709 840 SEC7.
 REGION 2 224 DCB; DCB:DCB domain and DCB:HUS domain
 REGION 557 577 HUS; DCB:HUS domain interaction.
 MOTIF 711 715 Nuclear localization signal (NLS).
 MOD_RES 1079 1079 Phosphoserine.
 MOD_RES 1569 1569 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Golgi apparatus; Guanine-nucleotide releasing factor; Membrane; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1849 AA 
Protein Sequence
MYEGKKTKNM FLTRALEKIL ADKEVKKAHH SQLRKACEVA LEEIKAETEK QSPPHGEAKA 60
GSSTLPPVKS KTNFIEADKY FLPFELACQS KCPRIVSTSL DCLQKLIAYG HLTGNAPDST 120
TPGKKLIDRI IETICGCFQG PQTDEGVQLQ IIKALLTAVT SQHIEIHEGT VLQAVRTCYN 180
IYLASKNLIN QTTAKATLTQ MLNVIFARME NQALQEAKQM EKERHRQHHH LLQSPVSHHE 240
PESPQLRYLP PQTVDHISQE HEGDLDLHTN DVDKSLQDDT EPENGSDISS AENEQTEADQ 300
ATAAETLSKN EVLYDGENHD CEEKPQDIVQ NIVEEMVNIV VGDMGEGTTI NASADGNIGT 360
IEDGSDSENI QANGIPGTPI SVAYTPSLPD DRLSVSSNDT QESGNSSGPS PGAKFSHILQ 420
KDAFLVFRSL CKLSMKPLSD GPPDPKSHEL RSKILSLQLL LSILQNAGPI FRTNEMFINA 480
IKQYLCVALS KNGVSSVPEV FELSLSIFLT LLSNFKTHLK MQIEVFFKEI FLYILETSTS 540
SFDHKWMVIQ TLTRICADAQ SVVDIYVNYD CDLNAANIFE RLVNDLSKIA QGRGSQELGM 600
SNVQELSLRK KGLECLVSIL KCMVEWSKDQ YVNPNSQTTL GQEKPSEQEM SEIKHPETIN 660
RYGSLNSLES TSSSGIGSYS TQMSGTDNPE QFEVLKQQKE IIEQGIDLFN KKPKRGIQYL 720
QEQGMLGTTP EDIAQFLHQE ERLDSTQVGE FLGDNDKFNK EVMYAYVDQH DFSGKDFVSA 780
LRMFLEGFRL PGEAQKIDRL MEKFAARYLE CNQGQTLFAS ADTAYVLAYS IIMLTTDLHS 840
PQVKNKMTKE QYIKMNRGIN DSKDLPEEYL SAIYNEIAGK KISMKETKEL TIPTKSSKQN 900
VASEKQRRLL YNLEMEQMAK TAKALMEAVS HVQAPFTSAT HLEHVRPMFK LAWTPFLAAF 960
SVGLQDCDDT EVASLCLEGI RCAIRIACIF SIQLERDAYV QALARFTLLT VSSGITEMKQ 1020
KNIDTIKTLI TVAHTDGNYL GNSWHEILKC ISQLELAQLI GTGVKPRYIS GTVRGREGSL 1080
TGTKDQAPDE FVGLGLVGGN VDWKQIASIQ ESIGETSSQS VVVAVDRIFT GSTRLDGNAI 1140
VDFVRWLCAV SMDELLSTTH PRMFSLQKIV EISYYNMGRI RLQWSRIWEV IGDHFNKVGC 1200
NPNEDVAIFA VDSLRQLSMK FLEKGELANF RFQKDFLRPF EHIMKRNRSP TIRDMVVRCI 1260
AQMVNSQAAN IRSGWKNIFS VFHLAASDQD ESIVELAFQT TGHIVTLVFE KHFPATIDSF 1320
QDAVKCLSEF ACNAAFPDTS MEAIRLIRHC AKYVSDRPQA FKEYTSDDMN VAPEDRVWVR 1380
GWFPILFELS CIINRCKLDV RTRGLTVMFE IMKTYGHTYE KHWWQDLFRI VFRIFDNMKL 1440
PEQQTEKAEW MTTTCNHALY AICDVFTQYL EVLSDVLLDD IFAQLYWCVQ QDNEQLARSG 1500
TNCLENVVIL NGEKFTLEIW DKTCNCTLDI FKTTIPHALL TWRPNSGETA PPPPSPVSEK 1560
PLDTISQKSV DIHDSIQPRS VDNRPQAPLV SASAVNEEVS KIKSTAKFPE QKLFAALLIK 1620
CVVQLELIQT IDNIVFFPAT SKKEDAENLA AAQRDAVDFD VRVDTQDQGM YRFLTSQQLF 1680
KLLDCLLESH RFAKAFNSNN EQRTALWKAG FKGKSKPNLL KQETSSLACG LRILFRMYMD 1740
ESRVSAWEEV QQRLLNVCSE ALSYFLTLTS ESHREAWTNL LLLFLTKVLK ISDNRFKAHA 1800
SFYYPLLCEI MQFDLIPELR AVLRRFFLRI GVVFQISQPP EQELGINKQ 1849 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0000139; C:Golgi membrane; IDA:UniProtKB.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0030532; C:small nuclear ribonucleoprotein complex; IDA:UniProtKB.
 GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
 GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IBA:RefGenome.
 GO:0034237; F:protein kinase A regulatory subunit binding; IDA:UniProtKB.
 GO:0010256; P:endomembrane system organization; IMP:UniProtKB.
 GO:0006887; P:exocytosis; TAS:ProtInc.
 GO:0007030; P:Golgi organization; IMP:UniProtKB.
 GO:0030837; P:negative regulation of actin filament polymerization; IMP:UniProtKB.
 GO:0034259; P:negative regulation of Rho GTPase activity; IDA:UniProtKB.
 GO:0090284; P:positive regulation of protein glycosylation in Golgi; IMP:UniProtKB.
 GO:0090303; P:positive regulation of wound healing; IMP:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
 GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR015403; DUF1981_SEC7_assoc.
 IPR000904; Sec7.
 IPR023394; SEC7_alpha_orthog. 
Pfam
 PF09324; DUF1981
 PF01369; Sec7 
SMART
 SM00222; Sec7 
PROSITE
 PS50190; SEC7 
PRINTS