CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000012
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Unconventional myosin-If 
Protein Synonyms/Alias
 Myosin-Ie 
Gene Name
 MYO1F 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
158LEAFGNAKTVRNNNSubiquitination[1, 2, 3, 4]
170NNSSRFGKYFEIQFSubiquitination[1]
194ISNFLLEKSRVVMQNubiquitination[1]
355YTRDALAKGLYARLFubiquitination[1]
611QVEYLGLKENIRVRRubiquitination[2, 3, 4]
673QYQMGSTKVFVKNPEubiquitination[1]
905FGDLAVLKVGGRTLTubiquitination[1]
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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
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 1 677 Myosin head-like.
 DOMAIN 693 722 IQ.
 DOMAIN 1041 1098 SH3.
 NP_BIND 110 117 ATP (Potential).
 REGION 579 589 Actin-binding (Potential).
 MOD_RES 734 734 Phosphoserine (By similarity).
 MOD_RES 1023 1023 Phosphoserine.  
Keyword
 Actin-binding; ATP-binding; Calmodulin-binding; Complete proteome; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1098 AA 
Protein Sequence
MGSKERFHWQ SHNVKQSGVD DMVLLPQITE DAIAANLRKR FMDDYIFTYI GSVLISVNPF 60
KQMPYFTDRE IDLYQGAAQY ENPPHIYALT DNMYRNMLID CENQCVIISG ESGAGKTVAA 120
KYIMGYISKV SGGGEKVQHV KDIILQSNPL LEAFGNAKTV RNNNSSRFGK YFEIQFSRGG 180
EPDGGKISNF LLEKSRVVMQ NENERNFHIY YQLLEGASQE QRQNLGLMTP DYYYYLNQSD 240
TYQVDGTDDR SDFGETLSAM QVIGIPPSIQ QLVLQLVAGI LHLGNISFCE DGNYARVESV 300
DLLAFPAYLL GIDSGRLQEK LTSRKMDSRW GGRSESINVT LNVEQAAYTR DALAKGLYAR 360
LFDFLVEAIN RAMQKPQEEY SIGVLDIYGF EIFQKNGFEQ FCINFVNEKL QQIFIELTLK 420
AEQEEYVQEG IRWTPIQYFN NKVVCDLIEN KLSPPGIMSV LDDVCATMHA TGGGADQTLL 480
QKLQAAVGTH EHFNSWSAGF VIHHYAGKVS YDVSGFCERN RDVLFSDLIE LMQTSEQAFL 540
RMLFPEKLDG DKKGRPSTAG SKIKKQANDL VATLMRCTPH YIRCIKPNET KRPRDWEENR 600
VKHQVEYLGL KENIRVRRAG FAYRRQFAKF LQRYAILTPE TWPRWRGDER QGVQHLLRAV 660
NMEPDQYQMG STKVFVKNPE SLFLLEEVRE RKFDGFARTI QKAWRRHVAV RKYEEMREEA 720
SNILLNKKER RRNSINRNFV GDYLGLEERP ELRQFLGKRE RVDFADSVTK YDRRFKPIKR 780
DLILTPKCVY VIGREKVKKG PEKGQVCEVL KKKVDIQALR GVSLSTRQDD FFILQEDAAD 840
SFLESVFKTE FVSLLCKRFE EATRRPLPLT FSDTLQFRVK KEGWGGGGTR SVTFSRGFGD 900
LAVLKVGGRT LTVSVGDGLP KSSKPTRKGM AKGKPRRSSQ APTRAAPAPP RGMDRNGVPP 960
SARGGPLPLE IMSGGGTHRP PRGPPSTSLG ASRRPRARPP SEHNTEFLNV PDQGMAGMQR 1020
KRSVGQRPVP GVGRPKPQPR THGPRCRALY QYVGQDVDEL SFNVNEVIEI LMEDPSGWWK 1080
GRLHGQEGLF PGNYVEKI 1098 
Gene Ontology
 GO:0030864; C:cortical actin cytoskeleton; IEA:Compara.
 GO:0031941; C:filamentous actin; IEA:Compara.
 GO:0016461; C:unconventional myosin complex; NAS:UniProtKB.
 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:0050830; P:defense response to Gram-positive bacterium; IEA:Compara.
 GO:0007162; P:negative regulation of cell adhesion; IEA:Compara.
 GO:0043312; P:neutrophil degranulation; IEA:Compara.
 GO:0030335; P:positive regulation of cell migration; IEA:Compara.
 GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Compara.
 GO:0045088; P:regulation of innate immune response; IEA:Compara. 
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
 SM00015; IQ
 SM00242; MYSc
 SM00326; SH3 
PROSITE
 PS50096; IQ
 PS50002; SH3 
PRINTS
 PR00193; MYOSINHEAVY.
 PR00452; SH3DOMAIN.