CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011959
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Unconventional myosin-Ie 
Protein Synonyms/Alias
 Myosin-Ic; Unconventional myosin 1E 
Gene Name
 MYO1E 
Gene Synonyms/Alias
 MYO1C 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
160LEAFGNAKTVRNNNSubiquitination[1]
444PIEYFNNKIVCDLIEubiquitination[1]
631AYRRIFQKFLQRYAIubiquitination[2]
1019PESLDFLKVPDQGAAubiquitination[3]
Reference
 [1] 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]
 [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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
 Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14. 
Sequence Annotation
 DOMAIN 1 679 Myosin head-like.
 DOMAIN 695 724 IQ.
 DOMAIN 1051 1108 SH3.
 NP_BIND 112 119 ATP (Potential).
 REGION 581 591 Actin-binding (Potential).
 MOD_RES 980 980 Phosphoserine.
 MOD_RES 1002 1002 Phosphoserine.  
Keyword
 Actin-binding; ATP-binding; Calmodulin-binding; Cell junction; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Disease mutation; Lipid-binding; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1108 AA 
Protein Sequence
MGSKGVYQYH WQSHNVKHSG VDDMVLLSKI TENSIVENLK KRYMDDYIFT YIGSVLISVN 60
PFKQMPYFGE KEIEMYQGAA QYENPPHIYA LADNMYRNMI IDRENQCVII SGESGAGKTV 120
AAKYIMSYIS RVSGGGTKVQ HVKDIILQSN PLLEAFGNAK TVRNNNSSRF GKYFEIQFSP 180
GGEPDGGKIS NFLLEKSRVV MRNPGERSFH IFYQLIEGAS AEQKHSLGIT SMDYYYYLSL 240
SGSYKVDDID DRREFQETLH AMNVIGIFAE EQTLVLQIVA GILHLGNISF KEVGNYAAVE 300
SEEFLAFPAY LLGINQDRLK EKLTSRQMDS KWGGKSESIH VTLNVEQACY TRDALAKALH 360
ARVFDFLVDS INKAMEKDHE EYNIGVLDIY GFEIFQKNGF EQFCINFVNE KLQQIFIELT 420
LKAEQEEYVQ EGIRWTPIEY FNNKIVCDLI ENKVNPPGIM SILDDVCATM HAVGEGADQT 480
LLQKLQMQIG SHEHFNSWNQ GFIIHHYAGK VSYDMDGFCE RNRDVLFMDL IELMQSSELP 540
FIKSLFPENL QADKKGRPTT AGSKIKKQAN DLVSTLMKCT PHYIRCIKPN ETKKPRDWEE 600
SRVKHQVEYL GLKENIRVRR AGYAYRRIFQ KFLQRYAILT KATWPSWQGE EKQGVLHLLQ 660
SVNMDSDQFQ LGRSKVFIKA PESLFLLEEM RERKYDGYAR VIQKSWRKFV ARKKYVQMRE 720
EASDLLLNKK ERRRNSINRN FIGDYIGMEE HPELQQFVGK REKIDFADTV TKYDRRFKGV 780
KRDLLLTPKC LYLIGREKVK QGPDKGLVKE VLKRKIEIER ILSVSLSTMQ DDIFILHEQE 840
YDSLLESVFK TEFLSLLAKR YEEKTQKQLP LKFSNTLELK LKKENWGPWS AGGSRQVQFH 900
QGFGDLAVLK PSNKVLQVSI GPGLPKNSRP TRRNTTQNTG YSSGTQNANY PVRAAPPPPG 960
YHQNGVIRNQ YVPYPHAPGS QRSNQKSLYT SMARPPLPRQ QSTSSDRVSQ TPESLDFLKV 1020
PDQGAAGVRR QTTSRPPPAG GRPKPQPKPK PQVPQCKALY AYDAQDTDEL SFNANDIIDI 1080
IKEDPSGWWT GRLRGKQGLF PNNYVTKI 1108 
Gene Ontology
 GO:0005912; C:adherens junction; ISS:UniProtKB.
 GO:0005911; C:cell-cell junction; ISS:UniProtKB.
 GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0016459; C:myosin complex; TAS:UniProtKB.
 GO:0051015; F:actin filament binding; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042623; F:ATPase activity, coupled; IDA:UniProtKB.
 GO:0005516; F:calmodulin binding; IDA:UniProtKB.
 GO:0000146; F:microfilament motor activity; TAS:UniProtKB.
 GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
 GO:0030048; P:actin filament-based movement; TAS:UniProtKB.
 GO:0006897; P:endocytosis; IMP:UniProtKB.
 GO:0032836; P:glomerular basement membrane development; ISS:UniProtKB.
 GO:0003094; P:glomerular filtration; ISS:UniProtKB.
 GO:0072015; P:glomerular visceral epithelial cell development; ISS:UniProtKB.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Compara.
 GO:0035166; P:post-embryonic hemopoiesis; IEA:Compara.
 GO:0001570; P:vasculogenesis; IEA:Compara. 
Interpro
 IPR000048; IQ_motif_EF-hand-BS.
 IPR001609; Myosin_head_motor_dom.
 IPR010926; Myosin_tail_2.
 IPR027417; P-loop_NTPase.
 IPR001452; SH3_domain. 
Pfam
 PF00063; Myosin_head
 PF06017; Myosin_TH1
 PF00018; SH3_1 
SMART
 SM00242; MYSc
 SM00326; SH3 
PROSITE
 PS50096; IQ
 PS50002; SH3 
PRINTS
 PR00193; MYOSINHEAVY.
 PR00452; SH3DOMAIN.