CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039475
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Myosin-14 
Protein Synonyms/Alias
  
Gene Name
 MYH14 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
252LEAFGNAKTVKNDNSubiquitination[1, 2, 3, 4, 5]
255FGNAKTVKNDNSSRFubiquitination[6]
429VGRDYVQKAQTKEQAacetylation[6]
429VGRDYVQKAQTKEQAubiquitination[2, 4, 6]
433YVQKAQTKEQADFALubiquitination[4]
566WFPKATDKSFVEKVAubiquitination[4]
788LTPNAIPKGFMDGKQubiquitination[1]
878RNCAAYLKLRHWQWWubiquitination[3, 4]
892WRLFTKVKPLLQVTRubiquitination[1]
913ARAQELQKVQELQQQubiquitination[1]
1023RQKLQLEKVTTEAKMacetylation[7]
1138LRAQLGRKEEELQAAacetylation[8]
1502TLEKKQRKFDQLLAEacetylation[6]
1502TLEKKQRKFDQLLAEubiquitination[1, 4]
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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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]
 [8] 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
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
 2028 AA 
Protein Sequence
MAAVTMSVPG RKAPPRPGPV PEAAQPFLFT PRGPSAGGGP GSGTSPQVEW TARRLVWVPS 60
ELHGFEAAAL RDEGEEEAEV ELAESGRRLR LPRDQIQRMN PPKFSKAEDM AELTCLNEAS 120
VLHNLRERYY SGLIYTYSGL FCVVINPYKQ LPIYTEAIVE MYRGKKRHEV PPHVYAVTEG 180
AYRSMLQDRE DQSILCTGES GAGKTENTKK VIQYLAHVAS SPKGRKEPGV PGELERQLLQ 240
ANPILEAFGN AKTVKNDNSS RFGKFIRINF DVAGYIVGAN IETYLLEKSR AIRQAKDECS 300
FHIFYQLLGG AGEQLKADLL LEPCSHYRFL TNGPSSSPGQ ERELFQETLE SLRVLGFSHE 360
EIISMLRMVS AVLQFGNIAL KRERNTDQAT MPDNTAAQKL CRLLGLGVTD FSRALLTPRI 420
KVGRDYVQKA QTKEQADFAL EALAKATYER LFRWLVLRLN RALDRSPRQG ASFLGILDIA 480
GFEIFQLNSF EQLCINYTNE KLQQLFNHTM FVLEQEEYQR EGIPWTFLDF GLDLQPCIDL 540
IERPANPPGL LALLDEECWF PKATDKSFVE KVAQEQGGHP KFQRPRHLRD QADFSVLHYA 600
GKVDYKANEW LMKNMDPLND NVAALLHQST DRLTAEIWKD EHGGFQQFSF LGSFPPSPPG 660
SAERCSSAIS PPGVEGIVGL EQVSSLGDGP PGGRPRRGMF RTVGQLYKES LSRLMATLSN 720
TNPSFVRCIV PNHEKRAGKL EPRLVLDQLR CNGVLEGIRI CRQGFPNRIL FQEFRQRYEI 780
LTPNAIPKGF MDGKQACEKM IQALELDPNL YRVGQSKIFF RAGVLAQLEE ERDLKVTDII 840
VSFQAAARGY LARRAFQKRQ QQQSALRVMQ RNCAAYLKLR HWQWWRLFTK VKPLLQVTRQ 900
DEVLQARAQE LQKVQELQQQ SAREVGELQG RVAQLEEERA RLAEQLRAEA ELCAEAEETR 960
GRLAARKQEL ELVVSELEAR VGEEEECSRQ MQTEKKRLQQ HIQELEAHLE AEEGARQKLQ 1020
LEKVTTEAKM KKFEEDLLLL EDQNSKLSKE RKLLEDRLAE FSSQAAEEEE KVKSLNKLRL 1080
KYEATIADME DRLRKEEKGR QELEKLKRRL DGESSELQEQ MVEQQQRAEE LRAQLGRKEE 1140
ELQAALARAE DEGGARAQLL KSLREAQAAL AEAQEDLESE RVARTKAEKQ RRDLGEELEA 1200
LRGELEDTLD STNAQQELRS KREQEVTELK KTLEEETRIH EAAVQELRQR HGQALGELAE 1260
QLEQARRGKG AWEKTRLALE AEVSELRAEL SSLQTARQEG EQRRRRLELQ LQEVQGRAGD 1320
GERARAEAAE KLQRAQAELE NVSGALNEAE SKTIRLSKEL SSTEAQLHDA QELLQEETRA 1380
KLALGSRVRA MEAEAAGLRE QLEEEAAARE RAGRELQTAQ AQLSEWRRRQ EEEAGALEAG 1440
EEARRRAARE AEALTQRLAE KTETVDRLER GRRRLQQELD DATMDLEQQR QLVSTLEKKQ 1500
RKFDQLLAEE KAAVLRAVEE RERAEAEGRE REARALSLTR ALEEEQEARE ELERQNRALR 1560
AELEALLSSK DDVGKSVHEL ERACRVAEQA ANDLRAQVTE LEDELTAAED AKLRLEVTVQ 1620
ALKTQHERDL QGRDEAGEER RRQLAKQLRD AEVERDEERK QRTLAVAARK KLEGELEELK 1680
AQMASAGQGK EEAVKQLRKM QAQMKELWRE VEETRTSREE IFSQNRESEK RLKGLEAEVL 1740
RLQEELAASD RARRQAQQDR DEMADEVANG NLSKAAILEE KRQLEGRLGQ LEEELEEEQS 1800
NSELLNDRYR KLLLQVESLT TELSAERSFS AKAESGRQQL ERQIQELRGR LGEEDAGARA 1860
RHKMTIAALE SKLAQAEEQL EQETRERILS GKLVRRAEKR LKEVVLQVEE ERRVADQLRD 1920
QLEKGNLRVK QLKRQLEEAE EEASRAQAGR RRLQRELEDV TESAESMNRE VTTLRNRLRR 1980
GPLTFTTRTV RQVFRLEEGV ASDEEAEEAQ PGSGPSPEPE GSPPAHPQ 2028 
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.
 IPR002928; Myosin_tail.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00063; Myosin_head
 PF02736; Myosin_N
 PF01576; Myosin_tail_1 
SMART
 SM00015; IQ
 SM00242; MYSc 
PROSITE
 PS50096; IQ 
PRINTS
 PR00193; MYOSINHEAVY.