CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023986
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Brefeldin A-inhibited guanine nucleotide-exchange protein 2 
Protein Synonyms/Alias
 Brefeldin A-inhibited GEP 2; ADP-ribosylation factor guanine nucleotide-exchange factor 2 
Gene Name
 ARFGEF2 
Gene Synonyms/Alias
 ARFGEP2; BIG2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17FVSRALEKILADKEVacetylation[1]
22LEKILADKEVKRPQHacetylation[1]
25ILADKEVKRPQHSQLacetylation[1]
1010QLIGTGVKTRYLSGSubiquitination[2]
1171LSMKFLEKGELANFRubiquitination[2, 3]
1181LANFRFQKDFLRPFEubiquitination[2]
1727TLKINDEKFKAHASMubiquitination[4]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] 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]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 654 785 SEC7.
 REGION 2 224 DCB; DCB:DCB domain and DCB:HUS domain
 REGION 508 528 HUS; DCB:HUS domain interaction.
 MOD_RES 214 214 Phosphoserine (By similarity).
 MOD_RES 218 218 Phosphoserine.
 MOD_RES 227 227 Phosphoserine.
 MOD_RES 277 277 Phosphoserine.
 MOD_RES 614 614 Phosphoserine.
 MOD_RES 616 616 Phosphothreonine (By similarity).
 MOD_RES 1525 1525 Phosphoserine.
 MOD_RES 1528 1528 Phosphoserine.
 MOD_RES 1782 1782 Phosphoserine.  
Keyword
 3D-structure; Cell junction; Cell projection; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Disease mutation; Endosome; Golgi apparatus; Guanine-nucleotide releasing factor; Membrane; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Synapse; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1785 AA 
Protein Sequence
MQESQTKSMF VSRALEKILA DKEVKRPQHS QLRRACQVAL DEIKAEIEKQ RLGTAAPPKA 60
NFIEADKYFL PFELACQSKS PRVVSTSLDC LQKLIAYGHI TGNAPDSGAP GKRLIDRIVE 120
TICSCFQGPQ TDEGVQLQII KALLTAVTSP HIEIHEGTIL QTVRTCYNIY LASKNLINQT 180
TAKATLTQML NVIFTRMENQ VLQEARELEK PIQSKPQSPV IQAAAVSPKF VRLKHSQAQS 240
KPTTPEKTDL TNGEHARSDS GKVSTENGDA PRERGSSLSG TDDGAQEVVK DILEDVVTSA 300
IKEAAEKHGL TEPERVLGEL ECQECAIPPG VDENSQTNGI ADDRQSLSSA DNLESDAQGH 360
QVAARFSHVL QKDAFLVFRS LCKLSMKPLG EGPPDPKSHE LRSKVVSLQL LLSVLQNAGP 420
VFRTHEMFIN AIKQYLCVAL SKNGVSSVPD VFELSLAIFL TLLSNFKMHL KMQIEVFFKE 480
IFLNILETST SSFEHRWMVI QTLTRICADA QCVVDIYVNY DCDLNAANIF ERLVNDLSKI 540
AQGRSGHELG MTPLQELSLR KKGLECLVSI LKCMVEWSKD LYVNPNHQTS LGQERLTDQE 600
IGDGKGLDMA RRCSVTSMES TVSSGTQTTV QDDPEQFEVI KQQKEIIEHG IELFNKKPKR 660
GIQFLQEQGM LGTSVEDIAQ FLHQEERLDS TQVGDFLGDS ARFNKEVMYA YVDQLDFCEK 720
EFVSALRTFL EGFRLPGEAQ KIDRLMEKFA ARYIECNQGQ TLFASADTAY VLAYSIIMLT 780
TDLHSPQVKN KMTKEQYIKM NRGINDSKDL PEEYLSSIYE EIEGKKIAMK ETKELTIATK 840
STKQNVASEK QRRLLYNLEM EQMAKTAKAL MEAVSHAKAP FTSATHLDHV RPMFKLVWTP 900
LLAAYSIGLQ NCDDTEVASL CLEGIRCAIR IACIFGMQLE RDAYVQALAR FSLLTASSSI 960
TEMKQKNIDT IKTLITVAHT DGNYLGNSWH EILKCISQLE LAQLIGTGVK TRYLSGSGRE 1020
REGSLKGHTL AGEEFMGLGL GNLVSGGVDK RQMASFQESV GETSSQSVVV AVDRIFTGST 1080
RLDGNAIVDF VRWLCAVSMD ELASPHHPRM FSLQKIVEIS YYNMNRIRLQ WSRIWHVIGD 1140
HFNKVGCNPN EDVAIFAVDS LRQLSMKFLE KGELANFRFQ KDFLRPFEHI MKKNRSPTIR 1200
DMAIRCIAQM VNSQAANIRS GWKNIFAVFH QAASDHDGNI VELAFQTTCH IVTTIFQHHF 1260
PAAIDSFQDA VKCLSEFACN AAFPDTSMEA IRLIRFCGKY VSERPRVLQE YTSDDMNVAP 1320
GDRVWVRGWF PILFELSCII NRCKLDVRTR GLTVMFEIMK SYGHTFEKHW WQDLFRIVFR 1380
IFDNMKLPEQ LSEKSEWMTT TCNHALYAIC DVFTQFYEAL NEVLLSDVFA QLQWCVKQDN 1440
EQLARSGTNC LENLVISNGE KFSPEVWDET CNCMLDIFKT TIPHVLLTWR PVGMEEDSSE 1500
KHLDVDLDRQ SLSSIDKNPS ERGQSQLSNP TDDSWKGRPY ANQKLFASLL IKCVVQLELI 1560
QTIDNIVFYP ATSKKEDAEH MVAAQQDTLD ADIHIETEDQ GMYKYMSSQH LFKLLDCLQE 1620
SHSFSKAFNS NYEQRTVLWR AGFKGKSKPN LLKQETSSLA CCLRILFRMY VDENRRDSWE 1680
EIQQRLLTVC SEALAYFITV NSESHREAWT SLLLLLLTKT LKINDEKFKA HASMYYPYLC 1740
EIMQFDLIPE LRAVLRKFFL RIGVVYKIWI PEEPSQVPAA LSPVW 1785 
Gene Ontology
 GO:0032279; C:asymmetric synapse; ISS:UniProtKB.
 GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
 GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
 GO:0005829; C:cytosol; IDA:MGI.
 GO:0043197; C:dendritic spine; ISS:UniProtKB.
 GO:0000139; C:Golgi membrane; IDA:UniProtKB.
 GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0055037; C:recycling endosome; IDA:UniProtKB.
 GO:0032280; C:symmetric synapse; ISS:UniProtKB.
 GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
 GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
 GO:0050811; F:GABA receptor binding; ISS:UniProtKB.
 GO:0034237; F:protein kinase A regulatory subunit binding; IDA:UniProtKB.
 GO:0010256; P:endomembrane system organization; IMP:UniProtKB.
 GO:0007032; P:endosome organization; IMP:UniProtKB.
 GO:0006887; P:exocytosis; TAS:ProtInc.
 GO:0006893; P:Golgi to plasma membrane transport; IMP:UniProtKB.
 GO:0035556; P:intracellular signal transduction; IDA:MGI.
 GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0001881; P:receptor recycling; IDA:UniProtKB.
 GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro. 
Interpro
 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