CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023476
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Unconventional myosin-Ic 
Protein Synonyms/Alias
 Myosin I beta; MMI-beta; MMIb 
Gene Name
 Myo1c 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
188LEAFGNAKTLRNDNSubiquitination[1]
269QSYLYLVKGQCAKVSacetylation[2]
281KVSSINDKSDWKVMRacetylation[2]
281KVSSINDKSDWKVMRubiquitination[1]
361THRKIIAKGEELLSPubiquitination[1]
383YARDALAKAVYSRTFubiquitination[1]
404INRSLASKDAESPSWacetylation[3]
404INRSLASKDAESPSWubiquitination[1]
486ICDLVEEKFKGIISIacetylation[3]
486ICDLVEEKFKGIISIubiquitination[1]
595KSELSDKKRPETVATubiquitination[1]
618LVEILRSKEPAYIRCubiquitination[1]
647VLIRHQVKYLGLMENacetylation[2]
740RRQSLATKIQAAWRGubiquitination[1]
868RSISPEWKQQLQQKAubiquitination[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]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4- containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes. 
Sequence Annotation
 DOMAIN 36 718 Myosin head-like.
 DOMAIN 734 757 IQ 1.
 DOMAIN 758 786 IQ 2.
 NP_BIND 140 147 ATP (Potential).
 REGION 927 938 PIP2-binding motif.
 MOD_RES 383 383 N6-methyllysine (By similarity).
 MOD_RES 408 408 Phosphoserine.  
Keyword
 Acetylation; Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Membrane; Methylation; Motor protein; mRNA transport; Myosin; Nuclear pore complex; Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat; Translocation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1063 AA 
Protein Sequence
MALQVELIPT GEIIRVVHPH RPCKLALGSD GVRVTMESAL TARDRVGVQD FVLLENFTSE 60
AAFIENLRRR FRENLIYTYI GPVLVSVNPY RDLQIYSRQH MERYRGVSFY EVPPHLFAVA 120
DTVYRALRTE RRDQAVMISG ESGAGKTEAT KRLLQFYAET CPAPERGGAV RDRLLQSNPV 180
LEAFGNAKTL RNDNSSRFGK YMDVQFDFKG APVGGHILSY LLEKSRVVHQ NHGERNFHVF 240
YQLLEGGEEE TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVMRKA LSVIDFTEDE 300
VEDLLSIVAS VLHLGNIHFA ADEDSNAQVT TENQLKYLTR LLGVEGTTLR EALTHRKIIA 360
KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVRKINRS LASKDAESPS WRSTTVLGLL 420
DIYGFEVFQH NSFEQFCINY CNEKLQQLFI ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC 480
DLVEEKFKGI ISILDEECLR PGEATDLTFL EKLEDTVKPH PHFLTHKLAD QKTRKSLDRG 540
EFRLLHYAGE VTYSVTGFLD KNNDLLFRNL KETMCSSMNP IMAQCFDKSE LSDKKRPETV 600
ATQFKMSLLQ LVEILRSKEP AYIRCIKPND AKQPGRFDEV LIRHQVKYLG LMENLRVRRA 660
GFAYRRKYEA FLQRYKSLCP ETWPMWAGRP QDGVAVLVRH LGYKPEEYKM GRTKIFIRFP 720
KTLFATEDSL EVRRQSLATK IQAAWRGFHW RQKFLRVKRS AICIQSWWRG TLGRRKAAKR 780
KWAAQTIRRL IRGFILRHSP RCPENAFFLD HVRASFLLNL RRQLPRNVLD TSWPTPPPAL 840
REASELLREL CMKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR 900
LGTEEISPRV LQSLGSEPIQ YAVPVVKYDR KGYKPRPRQL LLTPSAVVIV EDAKVKQRID 960
YANLTGISVS SLSDSLFVLH VQREDNKQKG DVVLQSDHVI ETLTKTALSA DRVNNININQ 1020
GSITFAGGPG RDGIIDFTSG SELLITKAKN GHLAVVAPRL NSR 1063 
Gene Ontology
 GO:0009925; C:basal plasma membrane; IEA:Compara.
 GO:0005903; C:brush border; IDA:MGI.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0031941; C:filamentous actin; IEA:Compara.
 GO:0016328; C:lateral plasma membrane; IEA:Compara.
 GO:0016020; C:membrane; TAS:UniProtKB.
 GO:0045121; C:membrane raft; IEA:Compara.
 GO:0045160; C:myosin I complex; IDA:MGI.
 GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0032420; C:stereocilium; IDA:MGI.
 GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
 GO:0003779; F:actin binding; NAS:UniProtKB.
 GO:0005524; F:ATP binding; NAS:UniProtKB.
 GO:0005516; F:calmodulin binding; NAS:UniProtKB.
 GO:0003774; F:motor activity; IEA:InterPro.
 GO:0005543; F:phospholipid binding; TAS:UniProtKB.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0038089; P:positive regulation of cell migration by vascular endothelial growth factor signaling pathway; IEA:Compara.
 GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Compara.
 GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; IEA:Compara.
 GO:0006612; P:protein targeting to membrane; IEA:Compara.
 GO:2000810; P:regulation of tight junction assembly; IEA:Compara.
 GO:0006810; P:transport; IDA:MGI. 
Interpro
 IPR000048; IQ_motif_EF-hand-BS.
 IPR001609; Myosin_head_motor_dom.
 IPR010926; Myosin_tail_2.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00612; IQ
 PF00063; Myosin_head
 PF06017; Myosin_TH1 
SMART
 SM00015; IQ
 SM00242; MYSc 
PROSITE
 PS50096; IQ 
PRINTS
 PR00193; MYOSINHEAVY.