CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-040766
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Myosin-10 
Protein Synonyms/Alias
  
Gene Name
 MYH10 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
34QADWTAKKLVWIPSEubiquitination[1]
68ELAENGKKAMVNKDDubiquitination[1]
248LESFGNAKTVKNDNSubiquitination[1, 2, 3, 4]
379FGNISFKKERNTDQAubiquitination[1]
458WLVHRINKALDRTKRacetylation[5]
578QEQGSHSKFQKPRQLubiquitination[1]
588KPRQLKDKADFCIIHacetylation[4]
636RFVAELWKDVDRIVGubiquitination[1]
705NHEKRAGKLDPHLVLacetylation[4]
705NHEKRAGKLDPHLVLubiquitination[1, 2, 4, 6]
760PKGFMDGKQACERMIubiquitination[1]
783LYRIGQSKIFFRAGVubiquitination[2]
833QQQLSALKVLQRNCAubiquitination[2]
856QWWRVFTKVKPLLQVubiquitination[2]
858WRVFTKVKPLLQVTRubiquitination[2]
1037QLAEEEEKAKNLAKIacetylation[4]
1257KELACEVKVLQQVKAacetylation[7]
1464QVASNLEKKQKKFDQacetylation[4]
1500EAREKETKALSLARAacetylation[4, 5]
1816QNKELKAKLQELEGAacetylation[4]
1816QNKELKAKLQELEGAubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
  
Sequence Annotation
  
Keyword
 Actin-binding; ATP-binding; Coiled coil; Complete proteome; Motor protein; Myosin; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1992 AA 
Protein Sequence
MAQRTGLEDP ERYLFVDRAV IYNPATQADW TAKKLVWIPS ERHGFEAASI KEERGDEVMV 60
ELAENGKKAM VNKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKDRYY SGLIYTYSGL 120
FCVVINPYKN LPIYSENIIE MYRGKKRHEM PPHIYAISES AYRCMLQDRE DQSILCTGES 180
GAGKTENTKK VIQYLAHVAS SHKGRKDHNI PQESPKPVKH QASALLYGEL ERQLLQANPI 240
LESFGNAKTV KNDNSSRFGK FIRINFDVTG YIVGANIETY LLEKSRAVRQ AKDERTFHIF 300
YQLLSGAGEH LKSDLLLEGF NNYRFLSNGY IPIPGQQDKD NFQETMEAMH IMGFSHEEIL 360
SMLKVVSSVL QFGNISFKKE RNTDQASMPE NTVAQKLCHL LGMNVMEFTR AILTPRIKVG 420
RDYVQKAQTK EQADFAVEAL AKATYERLFR WLVHRINKAL DRTKRQGASF IGILDIAGFE 480
IFELNSFEQL CINYTNEKLQ QLFNHTMFIL EQEEYQREGI EWNFIDFGLD LQPCIDLIER 540
PANPPGVLAL LDEECWFPKA TDKTFVEKLV QEQGSHSKFQ KPRQLKDKAD FCIIHYAGKV 600
DYKADEWLMK NMDPLNDNVA TLLHQSSDRF VAELWKDVDR IVGLDQVTGM TETAFGSAYK 660
TKKGMFRTVG QLYKESLTKL MATLRNTNPN FVRCIIPNHE KRAGKLDPHL VLDQLRCNGV 720
LEGIRICRQG FPNRIVFQEF RQRYEILTPN AIPKGFMDGK QACERMIRAL ELDPNLYRIG 780
QSKIFFRAGV LAHLEEERDL KITDIIIFFQ AVCRGYLARK AFAKKQQQLS ALKVLQRNCA 840
AYLKLRHWQW WRVFTKVKPL LQVTRQEEEL QAKDEELLKV KEKQTKVEGE LEEMERKHQQ 900
LLEEKNILAE QLQAETELFA EAEEMRARLA AKKQELEEIL HDLESRVEEE EERNQILQNE 960
KKKMQAHIQD LEEQLDEEEG ARQKLQLEKV TAEAKIKKME EEILLLEDQN SKFIKEKKLM 1020
EDRIAECSSQ LAEEEEKAKN LAKIRNKQEV MISDLEERLK KEEKTRQELE KAKRKLDGET 1080
TDLQDQIAEL QAQIDELKLQ LAKKEEELQG ALARGDDETL HKNNALKVVR ELQAQIAELQ 1140
EDFESEKASR NKAEKQKRDL SEELEALKTE LEDTLDTTAA QQELRTKREQ EVAELKKALE 1200
EETKNHEAQI QDMRQRHATA LEELSEQLEQ AKRFKANLEK NKQGLETDNK ELACEVKVLQ 1260
QVKAESEHKR KKLDAQVQEL HAKVSEGDRL RVELAEKASK LQNELDNVST LLEEAEKKGI 1320
KFAKDAASLE SQLQDTQELL QEETRQKLNL SSRIRQLEEE KNSLQEQQEE EEEARKNLEK 1380
QVLALQSQLA DTKKKVDDDL GTIESLEEAK KKLLKDAEAL SQRLEEKALA YDKLEKTKNR 1440
LQQELDDLTV DLDHQRQVAS NLEKKQKKFD QLLAEEKSIS ARYAEERDRA EAEAREKETK 1500
ALSLARALEE ALEAKEEFER QNKQLRADME DLMSSKDDVG KNVHELEKSK RALEQQVEEM 1560
RTQLEELEDE LQATEDAKLR LEVNMQAMKA QFERDLQTRD EQNEEKKRLL IKQVRELEAE 1620
LEDERKQRAL AVASKKKMEI DLKDLEAQIE AANKARDEVI KQLRKLQAQM KDYQRELEEA 1680
RASRDEIFAQ SKESEKKLKS LEAEILQLQE ELASSERARR HAEQERDELA DEITNSASGK 1740
SALLDEKRRL EARIAQLEEE LEEEQSNMEL LNDRFRKTTL QVDTLNAELA AERSAAQKSD 1800
NARQQLERQN KELKAKLQEL EGAVKSKFKA TISALEAKIG QLEEQLEQEA KERAAANKLV 1860
RRTEKKLKEI FMQVEDERRH ADQYKEQMEK ANARMKQLKR QLEEAEEEAT RANASRRKLQ 1920
RELDDATEAN EGLSREVSTL KNRLRRGGPI SFSSSRSGRR QLHLEGASLE LSDDDTESKT 1980
SDVNETQPPQ SE 1992 
Gene Ontology
 GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003774; F:motor activity; IEA:InterPro. 
Interpro
 IPR000048; IQ_motif_EF-hand-BS.
 IPR027401; Myosin-like_IQ_dom.
 IPR001609; Myosin_head_motor_dom.
 IPR004009; Myosin_N.
 IPR008989; Myosin_S1_N.
 IPR002928; Myosin_tail.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00612; IQ
 PF00063; Myosin_head
 PF02736; Myosin_N
 PF01576; Myosin_tail_1 
SMART
 SM00015; IQ
 SM00242; MYSc 
PROSITE
 PS50096; IQ 
PRINTS
 PR00193; MYOSINHEAVY.