CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001473
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Unconventional myosin-Id 
Protein Synonyms/Alias
  
Gene Name
 MYO1D 
Gene Synonyms/Alias
 KIAA0727 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
67RDTIEQYKGRELYERubiquitination[1]
108SGESGAGKTEASKYIubiquitination[2]
329TGRDIIDKQHTEQEAubiquitination[1]
478FLEALNSKLGKHAHFubiquitination[1]
559LSITEVTKRPLTAATubiquitination[3, 4, 5]
767VKWPSPPKVLRRFEEubiquitination[3, 5]
811VAAVEMLKGQRADLGubiquitination[3, 5]
976QCSLHGKKCTVSVETubiquitination[4]
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] 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] 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] 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]
 [5] 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] 
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). 
Sequence Annotation
 DOMAIN 2 682 Myosin head-like.
 DOMAIN 699 719 IQ 1.
 DOMAIN 721 741 IQ 2.
 NP_BIND 102 109 ATP (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 200 200 Phosphoserine.
 MOD_RES 536 536 Phosphotyrosine (By similarity).  
Keyword
 Acetylation; Actin-binding; ATP-binding; Calmodulin-binding; Complete proteome; Direct protein sequencing; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1006 AA 
Protein Sequence
MAEQESLEFG KADFVLMDTV SMPEFMANLR LRFEKGRIYT FIGEVVVSVN PYKLLNIYGR 60
DTIEQYKGRE LYERPPHLFA IADAAYKAMK RRSKDTCIVI SGESGAGKTE ASKYIMQYIA 120
AITNPSQRAE VERVKNMLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPIGGH 180
INNYLLEKSR VIVQQPGERS FHSFYQLLQG GSEQMLRSLH LQKSLSSYNY IHVGAQLKSS 240
INDAAEFRVV ADAMKVIGFK PEEIQTVYKI LAAILHLGNL KFVVDGDTPL IENGKVVSII 300
AELLSTKTDM VEKALLYRTV ATGRDIIDKQ HTEQEASYGR DAFAKAIYER LFCWIVTRIN 360
DIIEVKNYDT TIHGKNTVIG VLDIYGFEIF DNNSFEQFCI NYCNEKLQQL FIQLVLKQEQ 420
EEYQREGIPW KHIDYFNNQI IVDLVEQQHK GIIAILDDAC MNVGKVTDEM FLEALNSKLG 480
KHAHFSSRKL CASDKILEFD RDFRIRHYAG DVVYSVIGFI DKNKDTLFQD FKRLMYNSSN 540
PVLKNMWPEG KLSITEVTKR PLTAATLFKN SMIALVDNLA SKEPYYVRCI KPNDKKSPQI 600
FDDERCRHQV EYLGLLENVR VRRAGFAFRQ TYEKFLHRYK MISEFTWPNH DLPSDKEAVK 660
KLIERCGFQD DVAYGKTKIF IRTPRTLFTL EELRAQMLIR IVLFLQKVWR GTLARMRYKR 720
TKAALTIIRY YRRYKVKSYI HEVARRFHGV KTMRDYGKHV KWPSPPKVLR RFEEALQTIF 780
NRWRASQLIK SIPASDLPQV RAKVAAVEML KGQRADLGLQ RAWEGNYLAS KPDTPQTSGT 840
FVPVANELKR KDKYMNVLFS CHVRKVNRFS KVEDRAIFVT DRHLYKMDPT KQYKVMKTIP 900
LYNLTGLSVS NGKDQLVVFH TKDNKDLIVC LFSKQPTHES RIGELVGVLV NHFKSEKRHL 960
QVNVTNPVQC SLHGKKCTVS VETRLNQPQP DFTKNRSGFI LSVPGN 1006 
Gene Ontology
 GO:0030673; C:axolemma; IEA:Compara.
 GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
 GO:0005790; C:smooth endoplasmic reticulum; IEA:Compara.
 GO:0030898; F:actin-dependent ATPase activity; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000146; F:microfilament motor activity; IEA:Compara.
 GO:0010923; P:negative regulation of phosphatase activity; IDA: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.