CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024769
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Unconventional myosin-Ie 
Protein Synonyms/Alias
 Unconventional myosin 1E 
Gene Name
 Myo1e 
Gene Synonyms/Alias
 Myr3 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
160LEAFGNAKTVRNNNSubiquitination[1]
196ISNFLLEKSRVVMRNubiquitination[1]
554PENLQADKKGRPTTAubiquitination[1]
613QVEYLGLKENIRVRRubiquitination[1]
760ELQQFVGKREKIDFAubiquitination[1]
772DFADTVTKYDRRFKGubiquitination[1]
914AILKPSNKVLQVSIGubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
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 (By similarity). 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 (By similarity). 
Sequence Annotation
 DOMAIN 21 679 Myosin head-like.
 DOMAIN 695 724 IQ.
 DOMAIN 1050 1107 SH3.
 NP_BIND 112 119 ATP (Potential).
 REGION 581 591 Actin-binding (Potential).
 MOD_RES 1001 1001 Phosphoserine (By similarity).  
Keyword
 3D-structure; Actin-binding; ATP-binding; Calmodulin-binding; Cell junction; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Lipid-binding; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1107 AA 
Protein Sequence
MGSKGAYRYH WQSHNVKHSG VDDMVLLSKI TESSIVENLK KRYMDDYIFT YIGSVLISVN 60
PFKQMPYFGE KEVEMYQGAA QYENPPHIYA LADSMYRNMI IDRENQCVII SGESGAGKTV 120
AAKYIMSYVS RVSGGGPKVQ HVKDIILQSN PLLEAFGNAK TVRNNNSSRF GKYFEIQFSP 180
GGEPDGGKIS NFLLEKSRVV MRNPGERSFH IFYQLIEGAS PEQKQSLGIT SMDYYYYLSL 240
SGSYKVDDID DKRDFQETLH AMNVIGIFSE EQTLVLQIVA GILHLGNISF KEVGNYAAVE 300
SEEFLAFPAY LLGINQDRLK EKLTSRQMDS KWGGKSESIH VTLNVEQACY TRDALAKALH 360
ARVFDFLVDS INKAMEKDHE EYNIGVLDIY GFEIFQKNGF EQFCINFVNE KLQQIFIELT 420
LKAEQEEYVQ EGIRWTPIEY FNNKIVCDLI ESKVNPPGIM SILDDVCATM HAVGEGADQT 480
LLQKLQMQIG SHEHFNSWNQ GFIIHHYAGK VSYDMDGFCE RNRDVLFMDL IELMQSSELP 540
FIKSLFPENL QADKKGRPTT AGSKIKKQAN DLVSTLMKCT PHYIRCIKPN ETKKPKDWEE 600
SRVKHQVEYL GLKENIRVRR AGYAYRRVFQ KFLQRYAILT KATWPVWRGD EKQGVLHLLQ 660
SVNMDSDQFQ LGRSKVFIKA PESLFLLEEM RERKYDGYAR VIQKTWRKFV ARKKYVQMRE 720
EASDLLLNKK ERRRNSINRN FIGDYIGMEE RPELQQFVGK REKIDFADTV TKYDRRFKGV 780
KRDLLLTPKC LYLIGREKVK QGPDKGVVKE VLKRRIEVER ILSVSLSTMQ DDIFILHEQE 840
YDSLLESVFK TEFLSLLAKR YEEKTQKQLP LKFSNTLELK LKKENWGPWS AGGSRQVQFH 900
QGFGDLAILK PSNKVLQVSI GPGLPKNSRP TRRNTVTSRG YPGGTKNNYP MRAAPAPPGC 960
HQNGVIRNQF VPPPHAFGNQ RSNQKSLYTS MARPPLPRQQ STGSDRLSQT PESLDFLKVP 1020
DQGVAGVRRQ TSSRPPPAGG RPKPQPKPKP QVPQCKALYA YDAQDTDELS FNANDIIDII 1080
KEDPSGWWTG RLRGKQGLFP NNYVTKI 1107 
Gene Ontology
 GO:0005912; C:adherens junction; IDA:UniProtKB.
 GO:0005911; C:cell-cell junction; IDA:UniProtKB.
 GO:0045334; C:clathrin-coated endocytic vesicle; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005856; C:cytoskeleton; ISS:UniProtKB.
 GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
 GO:0051015; F:actin filament binding; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042623; F:ATPase activity, coupled; ISS:UniProtKB.
 GO:0005516; F:calmodulin binding; ISS:UniProtKB.
 GO:0003774; F:motor activity; IEA:InterPro.
 GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
 GO:0006897; P:endocytosis; ISS:UniProtKB.
 GO:0032836; P:glomerular basement membrane development; IMP:UniProtKB.
 GO:0003094; P:glomerular filtration; IMP:UniProtKB.
 GO:0072015; P:glomerular visceral epithelial cell development; IMP:UniProtKB.
 GO:0001701; P:in utero embryonic development; IMP:MGI.
 GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
 GO:0035166; P:post-embryonic hemopoiesis; IMP:MGI.
 GO:0001570; P:vasculogenesis; IMP:MGI. 
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.