CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023207
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Unconventional myosin-VI 
Protein Synonyms/Alias
 Unconventional myosin-6 
Gene Name
 MYO6 
Gene Synonyms/Alias
 KIAA0389 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
196LEAFGNAKTVRNNNSubiquitination[1]
334IGLDDEEKLDLFRVVacetylation[2]
425NARDALAKTVYSHLFubiquitination[3]
646SFISVGNKFKTQLNLubiquitination[1, 3]
648ISVGNKFKTQLNLLLubiquitination[1]
750GLNENDYKFGLTKVFubiquitination[3]
755DYKFGLTKVFFRPGKubiquitination[3]
782DHLAELVKRVNHWLTubiquitination[1]
886DTLMAKIKSTMMTQEubiquitination[1]
897MTQEQIQKEYDALVKubiquitination[1]
993EAQLARQKEEESQQQubiquitination[1]
1076GPAVLATKAAAGTKKubiquitination[1, 3, 4]
1090KYDLSKWKYAELRDTubiquitination[3]
1119EEFHRRLKVYHAWKSubiquitination[3]
1141ETEQRAPKSVTDYDFubiquitination[3]
1192IRPADQYKDPQSKKKubiquitination[1, 3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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] 
Functional Description
 Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells (By similarity). 
Sequence Annotation
 DOMAIN 1 759 Myosin head-like.
 DOMAIN 814 834 IQ.
 NP_BIND 151 158 ATP (Potential).
 REGION 273 317 Responsible for slow ATPase activity (By
 REGION 665 672 Actin-binding (Potential).
 REGION 782 810 Required for binding calmodulin (By
 REGION 1116 1118 Interaction with OPTN.
 MOD_RES 405 405 Phosphothreonine (By similarity).  
Keyword
 Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding; Cell membrane; Cell projection; Coated pit; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Deafness; Disease mutation; Endocytosis; Golgi apparatus; Hearing; Membrane; Motor protein; Myosin; Non-syndromic deafness; Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1294 AA 
Protein Sequence
MEDGKPVWAP HPTDGFQMGN IVDIGPDSLT IEPLNQKGKT FLALINQVFP AEEDSKKDVE 60
DNCSLMYLNE ATLLHNIKVR YSKDRIYTYV ANILIAVNPY FDIPKIYSSE AIKSYQGKSL 120
GTRPPHVFAI ADKAFRDMKV LKMSQSIIVS GESGAGKTEN TKFVLRYLTE SYGTGQDIDD 180
RIVEANPLLE AFGNAKTVRN NNSSRFGKFV EIHFNEKSSV VGGFVSHYLL EKSRICVQGK 240
EERNYHIFYR LCAGASEDIR EKLHLSSPDN FRYLNRGCTR YFANKETDKQ ILQNRKSPEY 300
LKAGSMKDPL LDDHGDFIRM CTAMKKIGLD DEEKLDLFRV VAGVLHLGNI DFEEAGSTSG 360
GCNLKNKSAQ SLEYCAELLG LDQDDLRVSL TTRVMLTTAG GTKGTVIKVP LKVEQANNAR 420
DALAKTVYSH LFDHVVNRVN QCFPFETSSY FIGVLDIAGF EYFEHNSFEQ FCINYCNEKL 480
QQFFNERILK EEQELYQKEG LGVNEVHYVD NQDCIDLIEA KLVGILDILD EENRLPQPSD 540
QHFTSAVHQK HKDHFRLTIP RKSKLAVHRN IRDDEGFIIR HFAGAVCYET TQFVEKNNDA 600
LHMSLESLIC ESRDKFIREL FESSTNNNKD TKQKAGKLSF ISVGNKFKTQ LNLLLDKLRS 660
TGASFIRCIK PNLKMTSHHF EGAQILSQLQ CSGMVSVLDL MQGGYPSRAS FHELYNMYKK 720
YMPDKLARLD PRLFCKALFK ALGLNENDYK FGLTKVFFRP GKFAEFDQIM KSDPDHLAEL 780
VKRVNHWLTC SRWKKVQWCS LSVIKLKNKI KYRAEACIKM QKTIRMWLCK RRHKPRIDGL 840
VKVGTLKKRL DKFNEVVSVL KDGKPEMNKQ IKNLEISIDT LMAKIKSTMM TQEQIQKEYD 900
ALVKSSEELL SALQKKKQQE EEAERLRRIQ EEMEKERKRR EEDEKRRRKE EEERRMKLEM 960
EAKRKQEEEE RKKREDDEKR IQAEVEAQLA RQKEEESQQQ AVLEQERRDR ELALRIAQSE 1020
AELISDEAQA DLALRRSLDS YPVSKNDGTR PKMTPEQMAK EMSEFLSRGP AVLATKAAAG 1080
TKKYDLSKWK YAELRDTINT SCDIELLAAC REEFHRRLKV YHAWKSKNKK RNTETEQRAP 1140
KSVTDYDFAP FLNNSPQQNP AAQIPARQRE IEMNRQQRFF RIPFIRPADQ YKDPQSKKKG 1200
WWYAHFDGPW IARQMELHPD KPPILLVAGK DDMEMCELNL EETGLTRKRG AEILPRQFEE 1260
IWERCGGIQY LQNAIESRQA RPTYATAMLQ SLLK 1294 
Gene Ontology
 GO:0030424; C:axon; IEA:Compara.
 GO:0005938; C:cell cortex; ISS:UniProtKB.
 GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016591; C:DNA-directed RNA polymerase II, holoenzyme; IDA:UniProtKB.
 GO:0031941; C:filamentous actin; IDA:UniProtKB.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0005765; C:lysosomal membrane; TAS:Reactome.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0031965; C:nuclear membrane; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0001726; C:ruffle; IDA:UniProtKB.
 GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
 GO:0016461; C:unconventional myosin complex; TAS:UniProtKB.
 GO:0051015; F:actin filament binding; IDA:UniProtKB.
 GO:0043531; F:ADP binding; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005516; F:calmodulin binding; ISS:UniProtKB.
 GO:0060001; F:minus-end directed microfilament motor activity; NAS:UniProtKB.
 GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
 GO:0042491; P:auditory receptor cell differentiation; IEA:Compara.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0071257; P:cellular response to electrical stimulus; IEA:Compara.
 GO:0016358; P:dendrite development; IEA:Compara.
 GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IDA:UniProtKB.
 GO:0006897; P:endocytosis; IMP:UniProtKB.
 GO:0014047; P:glutamate secretion; IEA:Compara.
 GO:0042472; P:inner ear morphogenesis; IEA:Compara.
 GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
 GO:0007626; P:locomotory behavior; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
 GO:0006605; P:protein targeting; IEA:Compara.
 GO:0051046; P:regulation of secretion; IMP:UniProtKB.
 GO:0048167; P:regulation of synaptic plasticity; IEA:Compara.
 GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
 GO:0007416; P:synapse assembly; IEA:Compara.
 GO:0007268; P:synaptic transmission; TAS:Reactome. 
Interpro
 IPR000048; IQ_motif_EF-hand-BS.
 IPR001609; Myosin_head_motor_dom.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00063; Myosin_head 
SMART
 SM00015; IQ
 SM00242; MYSc 
PROSITE
 PS50096; IQ 
PRINTS
 PR00193; MYOSINHEAVY.