CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000010
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
188LEAFGNAKTLRNDNSubiquitination[1, 2, 3, 4]
285INDKSDWKVVRKALTacetylation[5]
361THRKIIAKGEELLSPubiquitination[2]
383YARDALAKAVYSRTFmethylation[6]
404INRSLASKDVESPSWubiquitination[1, 2, 3]
618LVEILQSKEPAYVRCubiquitination[3]
647VLIRHQVKYLGLLENacetylation[5]
647VLIRHQVKYLGLLENubiquitination[3]
704LVRHLGYKPEEYKMGacetylation[5]
721KIFIRFPKTLFATEDubiquitination[1]
740RRQSLATKIQAAWRGubiquitination[1, 3]
868RSISPEWKQQLQQKAubiquitination[1, 3]
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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681] 
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. 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 (By similarity). 
Sequence Annotation
 DOMAIN 36 718 Myosin head-like.
 DOMAIN 734 757 IQ 1.
 DOMAIN 758 786 IQ 2.
 NP_BIND 140 147 ATP (Potential).
 MOD_RES 383 383 N6-methyllysine.
 MOD_RES 408 408 Phosphoserine.  
Keyword
 Acetylation; Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Direct protein sequencing; Membrane; Methylation; Motor protein; mRNA transport; Myosin; Nuclear pore complex; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Repeat; Translocation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1063 AA 
Protein Sequence
MALQVELVPT 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 NHGERNFHIF 240
YQLLEGGEEE TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVVRKA LTVIDFTEDE 300
VEDLLSIVAS VLHLGNIHFA ANEESNAQVT TENQLKYLTR LLSVEGSTLR EALTHRKIIA 360
KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVGKINRS LASKDVESPS WRSTTVLGLL 420
DIYGFEVFQH NSFEQFCINY CNEKLQQLFI ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC 480
DLVEEKFKGI ISILDEECLR PGEATDLTFL EKLEDTVKHH PHFLTHKLAD QRTRKSLGRG 540
EFRLLHYAGE VTYSVTGFLD KNNDLLFRNL KETMCSSKNP IMSQCFDRSE LSDKKRPETV 600
ATQFKMSLLQ LVEILQSKEP AYVRCIKPND AKQPGRFDEV LIRHQVKYLG LLENLRVRRA 660
GFAYRRKYEA FLQRYKSLCP ETWPTWAGRP QDGVAVLVRH LGYKPEEYKM GRTKIFIRFP 720
KTLFATEDAL EVRRQSLATK IQAAWRGFHW RQKFLRVKRS AICIQSWWRG TLGRRKAAKR 780
KWAAQTIRRL IRGFVLRHAP RCPENAFFLD HVRTSFLLNL RRQLPQNVLD TSWPTPPPAL 840
REASELLREL CIKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR 900
LGTDEISPRV LQALGSEPIQ YAVPVVKYDR KGYKPRSRQL LLTPNAVVIV EDAKVKQRID 960
YANLTGISVS SLSDSLFVLH VQRADNKQKG DVVLQSDHVI ETLTKTALSA NRVNSININQ 1020
GSITFAGGPG RDGTIDFTPG SELLITKAKN GHLAVVAPRL NSR 1063 
Gene Ontology
 GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
 GO:0005903; C:brush border; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0031941; C:filamentous actin; IDA:UniProtKB.
 GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
 GO:0045121; C:membrane raft; IDA:UniProtKB.
 GO:0005902; C:microvillus; IDA:UniProtKB.
 GO:0045160; C:myosin I complex; IEA:Compara.
 GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
 GO:0016461; C:unconventional myosin complex; TAS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003774; F:motor activity; IEA:InterPro.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0038089; P:positive regulation of cell migration by vascular endothelial growth factor signaling pathway; IMP:UniProtKB.
 GO:0090314; P:positive regulation of protein targeting to membrane; IMP:UniProtKB.
 GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; IMP:UniProtKB.
 GO:0006612; P:protein targeting to membrane; IDA:UniProtKB.
 GO:2000810; P:regulation of tight junction assembly; IMP:UniProtKB. 
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.