CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019607
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Formin-binding protein 1 
Protein Synonyms/Alias
 Formin-binding protein 17; hFBP17 
Gene Name
 FNBP1 
Gene Synonyms/Alias
 FBP17; KIAA0554 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
27WGIDILEKYIKFVKEacetylation[1]
44EIELSYAKQLRNLSKubiquitination[2]
66SKEEEEYKYTSCKAFacetylation[1]
110ARYVQELKQERKSNFacetylation[1]
110ARYVQELKQERKSNFubiquitination[2]
122SNFHDGRKAQQHIETubiquitination[2]
132QHIETCWKQLESSKRacetylation[1]
166DADINVTKADVEKARubiquitination[3]
187HQMAEDSKADYSSILubiquitination[2]
232VRMGESMKTYAEVDRubiquitination[2, 4]
247QVIPIIGKCLDGIVKubiquitination[2]
292EDYTQPMKRTVSDNSubiquitination[2, 3, 4]
312GEGKPDLKFGGKSKGubiquitination[2]
320FGGKSKGKLWPFIKKubiquitination[5, 6]
326GKLWPFIKKNKLMSLubiquitination[4, 5, 6]
612YVEVCLDKNAKDS**ubiquitination[2]
Reference
 [1] 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]
 [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] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] 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]
 [6] 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] 
Functional Description
 May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL. 
Sequence Annotation
 DOMAIN 1 65 FCH.
 REPEAT 416 491 REM.
 DOMAIN 550 611 SH3.
 REGION 1 335 Interaction with microtubules (By
 REGION 1 288 F-BAR domain.
 REGION 1 79 Required for self-association and
 REGION 251 617 Required for self-association and
 REGION 400 552 Interaction with RND2 (By similarity).
 REGION 495 617 Interaction with PDE6G (By similarity).
 REGION 514 617 Required for interaction with TNKS.
 REGION 535 617 Interaction with DNM1 and DNM3.
 REGION 550 617 Interaction with ARHGAP17, DAAM1, DIAPH1
 REGION 553 610 Interaction with FASLG.
 REGION 553 609 Interaction with DNM2 and WASL.
 MOD_RES 66 66 N6-acetyllysine.
 MOD_RES 110 110 N6-acetyllysine.
 MOD_RES 294 294 Phosphothreonine (By similarity).
 MOD_RES 296 296 Phosphoserine.
 MOD_RES 299 299 Phosphoserine.
 MOD_RES 349 349 Phosphoserine.
 MOD_RES 359 359 Phosphoserine.
 MOD_RES 497 497 Phosphoserine (By similarity).
 MOD_RES 500 500 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell membrane; Chromosomal rearrangement; Coated pit; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Lipid-binding; Lysosome; Membrane; Phosphoprotein; Polymorphism; Reference proteome; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 617 AA 
Protein Sequence
MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK 60
EEEEYKYTSC KAFISNLNEM NDYAGQHEVI SENMASQIIV DLARYVQELK QERKSNFHDG 120
RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRH 180
QMAEDSKADY SSILQKFNHE QHEYYHTHIP NIFQKIQEME ERRIVRMGES MKTYAEVDRQ 240
VIPIIGKCLD GIVKAAESID QKNDSQLVIE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL 300
SNSRGEGKPD LKFGGKSKGK LWPFIKKNKL MSLLTSPHQP PPPPPASASP SAVPNGPQSP 360
KQQKEPLSHR FNEFMTSKPK IHCFRSLKRG LSLKLGATPE DFSNLPPEQR RKKLQQKVDE 420
LNKEIQKEMD QRDAITKMKD VYLKNPQMGD PASLDHKLAE VSQNIEKLRV ETQKFEAWLA 480
EVEGRLPARS EQARRQSGLY DSQNPPTVNN CAQDRESPDG SYTEEQSQES EMKVLATDFD 540
DEFDDEEPLP AIGTCKALYT FEGQNEGTIS VVEGETLYVI EEDKGDGWTR IRRNEDEEGY 600
VPTSYVEVCL DKNAKDS 617 
Gene Ontology
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
 GO:0006897; P:endocytosis; IEA:UniProtKB-KW. 
Interpro
 IPR001060; FCH_dom.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR001452; SH3_domain. 
Pfam
 PF00611; FCH
 PF00018; SH3_1 
SMART
 SM00055; FCH
 SM00326; SH3 
PROSITE
 PS50133; FCH
 PS50002; SH3 
PRINTS