CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022450
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myoferlin 
Protein Synonyms/Alias
 Fer-1-like protein 3 
Gene Name
 MYOF 
Gene Synonyms/Alias
 FER1L3; KIAA1207 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
102QSRSLPYKLISLLNEubiquitination[1, 2, 3, 4]
167AVRGPGPKGPVGTVSubiquitination[2]
527YDELNTGKGEGVAYRubiquitination[2]
712TLPLTEGKANVTVLDubiquitination[2]
884SGLVGRHKFSDVTGKacetylation[5]
1109TTEDGDEKSLEKQKHubiquitination[2]
1223FDNDQVGKDEFLGRSubiquitination[2]
1237SIFSPVVKLNSEMDIubiquitination[2]
1436VIEMEDTKPLLASKLubiquitination[2]
1477YIQKGYSKLKIYNCEacetylation[6]
1507TFKLYRGKSDENEDPubiquitination[2]
1805KDVILDEKSITGEEMubiquitination[2]
1818EMSDIYVKGWIPGNEubiquitination[2]
1928LDMIPDLKAMNPLKAubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] 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]
 [5] 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]
 [6] 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
Functional Description
 Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR (By similarity). 
Sequence Annotation
 DOMAIN 1 85 C2 1.
 DOMAIN 186 281 C2 2.
 DOMAIN 345 458 C2 3.
 DOMAIN 1126 1231 C2 4.
 DOMAIN 1538 1638 C2 5.
 REGION 186 281 Necessary for interaction with EHD2.
 MOD_RES 174 174 Phosphoserine.
 MOD_RES 884 884 N6-acetyllysine.
 MOD_RES 1915 1915 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell membrane; Complete proteome; Cytoplasmic vesicle; Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2061 AA 
Protein Sequence
MLRVIVESAS NIPKTKFGKP DPIVSVIFKD EKKKTKKVDN ELNPVWNEIL EFDLRGIPLD 60
FSSSLGIIVK DFETIGQNKL IGTATVALKD LTGDQSRSLP YKLISLLNEK GQDTGATIDL 120
VIGYDPPSAP HPNDLSGPSV PGMGGDGEED EGDEDRLDNA VRGPGPKGPV GTVSEAQLAR 180
RLTKVKNSRR MLSNKPQDFQ IRVRVIEGRQ LSGNNIRPVV KVHVCGQTHR TRIKRGNNPF 240
FDELFFYNVN MTPSELMDEI ISIRVYNSHS LRADCLMGEF KIDVGFVYDE PGHAVMRKWL 300
LLNDPEDTSS GSKGYMKVSM FVLGTGDEPP PERRDRDNDS DDVESNLLLP AGIALRWVTF 360
LLKIYRAEDI PQMDDAFSQT VKEIFGGNAD KKNLVDPFVE VSFAGKKVCT NIIEKNANPE 420
WNQVVNLQIK FPSVCEKIKL TIYDWDRLTK NDVVGTTYLH LSKIAASGGE VEDFSSSGTG 480
AASYTVNTGE TEVGFVPTFG PCYLNLYGSP REYTGFPDPY DELNTGKGEG VAYRGRILVE 540
LATFLEKTPP DKKLEPISND DLLVVEKYQR RRKYSLSAVF HSATMLQDVG EAIQFEVSIG 600
NYGNKFDTTC KPLASTTQYS RAVFDGNYYY YLPWAHTKPV VTLTSYWEDI SHRLDAVNTL 660
LAMAERLQTN IEALKSGIQG KIPANQLAEL WLKLIDEVIE DTRYTLPLTE GKANVTVLDT 720
QIRKLRSRSL SQIHEAAVRM RSEATDVKST LAEIEDWLDK LMQLTEEPQN SMPDIIIWMI 780
RGEKRLAYAR IPAHQVLYST SGENASGKYC GKTQTIFLKY PQEKNNGPKV PVELRVNIWL 840
GLSAVEKKFN SFAEGTFTVF AEMYENQALM FGKWGTSGLV GRHKFSDVTG KIKLKREFFL 900
PPKGWEWEGE WIVDPERSLL TEADAGHTEF TDEVYQNESR YPGGDWKPAE DTYTDANGDK 960
AASPSELTCP PGWEWEDDAW SYDINRAVDE KGWEYGITIP PDHKPKSWVA AEKMYHTHRR 1020
RRLVRKRKKD LTQTASSTAR AMEELQDQEG WEYASLIGWK FHWKQRSSDT FRRRRWRRKM 1080
APSETHGAAA IFKLEGALGA DTTEDGDEKS LEKQKHSATT VFGANTPIVS CNFDRVYIYH 1140
LRCYVYQARN LLALDKDSFS DPYAHICFLH RSKTTEIIHS TLNPTWDQTI IFDEVEIYGE 1200
PQTVLQNPPK VIMELFDNDQ VGKDEFLGRS IFSPVVKLNS EMDITPKLLW HPVMNGDKAC 1260
GDVLVTAELI LRGKDGSNLP ILPPQRAPNL YMVPQGIRPV VQLTAIEILA WGLRNMKNFQ 1320
MASITSPSLV VECGGERVES VVIKNLKKTP NFPSSVLFMK VFLPKEELYM PPLVIKVIDH 1380
RQFGRKPVVG QCTIERLDRF RCDPYAGKED IVPQLKASLL SAPPCRDIVI EMEDTKPLLA 1440
SKLTEKEEEI VDWWSKFYAS SGEHEKCGQY IQKGYSKLKI YNCELENVAE FEGLTDFSDT 1500
FKLYRGKSDE NEDPSVVGEF KGSFRIYPLP DDPSVPAPPR QFRELPDSVP QECTVRIYIV 1560
RGLELQPQDN NGLCDPYIKI TLGKKVIEDR DHYIPNTLNP VFGRMYELSC YLPQEKDLKI 1620
SVYDYDTFTR DEKVGETIID LENRFLSRFG SHCGIPEEYC VSGVNTWRDQ LRPTQLLQNV 1680
ARFKGFPQPI LSEDGSRIRY GGRDYSLDEF EANKILHQHL GAPEERLALH ILRTQGLVPE 1740
HVETRTLHST FQPNISQGKL QMWVDVFPKS LGPPGPPFNI TPRKAKKYYL RVIIWNTKDV 1800
ILDEKSITGE EMSDIYVKGW IPGNEENKQK TDVHYRSLDG EGNFNWRFVF PFDYLPAEQL 1860
CIVAKKEHFW SIDQTEFRIP PRLIIQIWDN DKFSLDDYLG FLELDLRHTI IPAKSPEKCR 1920
LDMIPDLKAM NPLKAKTASL FEQKSMKGWW PCYAEKDGAR VMAGKVEMTL EILNEKEADE 1980
RPAGKGRDEP NMNPKLDLPN RPETSFLWFT NPCKTMKFIV WRRFKWVIIG LLFLLILLLF 2040
VAVLLYSLPN YLSMKIVKPN V 2061 
Gene Ontology
 GO:0005901; C:caveola; ISS:UniProtKB.
 GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
 GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005635; C:nuclear envelope; TAS:ProtInc.
 GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
 GO:0005543; F:phospholipid binding; IDA:UniProtKB.
 GO:0008015; P:blood circulation; TAS:ProtInc.
 GO:0034605; P:cellular response to heat; IEA:Compara.
 GO:0006936; P:muscle contraction; TAS:ProtInc.
 GO:0001778; P:plasma membrane repair; ISS:UniProtKB.
 GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IEA:Compara. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR018029; C2_membr_targeting.
 IPR012968; FerIin-domain.
 IPR012560; Ferlin_A-domain.
 IPR012561; Ferlin_B-domain.
 IPR006614; Peroxin/Ferlin. 
Pfam
 PF00168; C2
 PF08165; FerA
 PF08150; FerB
 PF08151; FerI 
SMART
 SM00239; C2
 SM00694; DysFC
 SM00693; DysFN 
PROSITE
 PS50004; C2 
PRINTS