CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018163
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myosin-9 
Protein Synonyms/Alias
 Cellular myosin heavy chain, type A; Myosin heavy chain 9; Myosin heavy chain, non-muscle IIa; Non-muscle myosin heavy chain A; NMMHC-A; Non-muscle myosin heavy chain IIa; NMMHC II-a; NMMHC-IIA 
Gene Name
 Myh9 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
29AQADWAAKKLVWVPSubiquitination[1]
30QADWAAKKLVWVPSSubiquitination[1]
79IQKMNPPKFSKVEDMubiquitination[1]
139EEIVEMYKGKKRHEMacetylation[2]
139EEIVEMYKGKKRHEMubiquitination[1]
186GKTENTKKVIQYLAHubiquitination[1]
225LEAFGNAKTVKNDNSubiquitination[1]
299LLLEPYNKYRFLSNGacetylation[3, 4]
299LLLEPYNKYRFLSNGsuccinylation[4]
299LLLEPYNKYRFLSNGubiquitination[1]
316TIPGQQDKDMFQETMubiquitination[1]
355QLGNIAFKKERNTDQubiquitination[1]
373PDNTAAQKVSHLLGIubiquitination[1]
540WFPKATDKSFVEKVVubiquitination[1]
545TDKSFVEKVVQEQGTacetylation[2]
545TDKSFVEKVVQEQGTubiquitination[1]
555QEQGTHPKFQKPKQLubiquitination[1]
580YAGKVDYKADEWLMKubiquitination[1]
613KFVSELWKDVDRIIGacetylation[2, 4]
637TALPGAFKTRKGMFRubiquitination[1]
651RTVGQLYKEQLAKLMacetylation[2, 4, 5]
651RTVGQLYKEQLAKLMsuccinylation[4]
656LYKEQLAKLMATLRNacetylation[2, 4]
656LYKEQLAKLMATLRNsuccinylation[4]
682NHEKKAGKLDPHLVLubiquitination[1]
737PKGFMDGKQACVLMIacetylation[2]
760LYRIGQSKVFFRAGVubiquitination[1]
835WRLFTKVKPLLNSIRubiquitination[1]
850HEDELLAKEAELTKVacetylation[2, 4]
850HEDELLAKEAELTKVsuccinylation[4]
860ELTKVREKHLAAENRacetylation[4]
860ELTKVREKHLAAENRubiquitination[1]
910RARLTAKKQELEEICacetylation[4]
975TTEAKLKKLEEDQIIacetylation[4]
1014NLMEEEEKSKSLAKLacetylation[3, 4]
1024SLAKLKNKHEAMITDacetylation[2, 4]
1099VEEEAAQKNMALKKIacetylation[4]
1099VEEEAAQKNMALKKIsuccinylation[4]
1181KTLEDEAKTHEAQIQacetylation[2]
1193QIQEMRQKHSQAVEEacetylation[2]
1209ADQLEQTKRVKATLEacetylation[2, 4]
1209ADQLEQTKRVKATLEsuccinylation[4]
1234GELANEVKALLQGKGacetylation[2]
1249DSEHKRKKVEAQLQEacetylation[2, 3, 4]
1249DSEHKRKKVEAQLQEsuccinylation[4]
1274VRTELADKVTKLQVEubiquitination[1]
1330QKLSLSTKLKQMEDEacetylation[4]
1330QKLSLSTKLKQMEDEsuccinylation[4]
1357EAKRNLEKQIATLHAacetylation[4]
1357EAKRNLEKQIATLHAsuccinylation[4]
1372QVTDMKKKMEDGVGCacetylation[2, 4]
1372QVTDMKKKMEDGVGCsuccinylation[4]
1392EAKRRLQKDLEGLSQacetylation[2, 4]
1392EAKRRLQKDLEGLSQsuccinylation[4]
1392EAKRRLQKDLEGLSQubiquitination[1]
1404LSQRLEEKVAAYDKLacetylation[2, 4, 6]
1404LSQRLEEKVAAYDKLsuccinylation[4]
1410EKVAAYDKLEKTKTRacetylation[2, 4]
1410EKVAAYDKLEKTKTRsuccinylation[4]
1413AAYDKLEKTKTRLQQubiquitination[1]
1454DQLLAEEKTISAKYAacetylation[2, 4]
1454DQLLAEEKTISAKYAsuccinylation[4]
1459EEKTISAKYAEERDRacetylation[2, 4]
1492LEEAMEQKAELERLNacetylation[2]
1513MEDLMSSKDDVGKSVacetylation[4]
1525KSVHELEKSKRALEQacetylation[2, 4]
1638KNREEAIKQLRKLQAacetylation[2]
1669EEILAQAKENEKKLKacetylation[4]
1669EEILAQAKENEKKLKsuccinylation[4]
1754LINDRLKKANLQIDQacetylation[4]
1754LINDRLKKANLQIDQsuccinylation[4]
1775LERSHAQKNENARQQacetylation[6, 7]
1793QNKELKAKLQEMESAacetylation[4]
1793QNKELKAKLQEMESAsuccinylation[4]
1802QEMESAVKSKYKASIacetylation[4]
1802QEMESAVKSKYKASIsuccinylation[4]
1806SAVKSKYKASIAALEacetylation[4]
1806SAVKSKYKASIAALEsuccinylation[4]
1845RRTEKKLKDVLLQVEacetylation[2, 4]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] 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]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [6] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [7] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 
Functional Description
 Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Plays a role in cell spreading and cell migration. 
Sequence Annotation
 DOMAIN 2 778 Myosin head-like.
 DOMAIN 779 808 IQ.
 NP_BIND 174 181 ATP (Potential).
 REGION 654 676 Actin-binding.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 8 8 N6-acetyllysine (By similarity).
 MOD_RES 11 11 Phosphotyrosine (By similarity).
 MOD_RES 102 102 N6-acetyllysine (By similarity).
 MOD_RES 181 181 Phosphothreonine.
 MOD_RES 299 299 N6-acetyllysine (By similarity).
 MOD_RES 754 754 Phosphotyrosine.
 MOD_RES 1024 1024 N6-acetyllysine (By similarity).
 MOD_RES 1357 1357 N6-acetyllysine (By similarity).
 MOD_RES 1392 1392 N6-acetyllysine (By similarity).
 MOD_RES 1404 1404 N6-acetyllysine (By similarity).
 MOD_RES 1410 1410 N6-acetyllysine (By similarity).
 MOD_RES 1459 1459 N6-acetyllysine (By similarity).
 MOD_RES 1638 1638 N6-acetyllysine (By similarity).
 MOD_RES 1714 1714 Phosphoserine (By similarity).
 MOD_RES 1939 1939 Phosphothreonine.
 MOD_RES 1943 1943 Phosphoserine.  
Keyword
 Acetylation; Actin-binding; ATP-binding; Calmodulin-binding; Cell shape; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1960 AA 
Protein Sequence
MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSSKNG FEPASLKEEV GEEAIVELVE 60
NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN LKERYYSGLI YTYSGLFCVV 120
INPYKNLPIY SEEIVEMYKG KKRHEMPPHI YAITDTAYRS MMQDREDQSI LCTGESGAGK 180
TENTKKVIQY LAHVASSHKS KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR 240
INFDVNGYIV GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY 300
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEDEQMGLL RVISGVLQLG NIAFKKERNT 360
DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY VQKAQTKEQA DFAIEALAKA 420
TYERMFRWLV LRINKALDKT KRQGASFIGI LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF 480
NHTMFILEQE EYQREGIEWN FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK 540
SFVEKVVQEQ GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL 600
HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY KEQLAKLMAT 660
LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG IRICRQGFPN RVVFQEFRQR 720
YEILTPNSIP KGFMDGKQAC VLMIKALELD SNLYRIGQSK VFFRAGVLAH LEEERDLKIT 780
DVIIGFQACC RGYLARKAFA KRQQQLTAMK VLQRNCAAYL RLRNWQWWRL FTKVKPLLNS 840
IRHEDELLAK EAELTKVREK HLAAENRLTE METMQSQLMA EKLQLQEQLQ AETELCAEAE 900
ELRARLTAKK QELEEICHDL EARVEEEEER CQYLQAEKKK MQQNIQELEE QLEEEESARQ 960
KLQLEKVTTE AKLKKLEEDQ IIMEDQNCKL AKEKKLLEDR VAEFTTNLME EEEKSKSLAK 1020
LKNKHEAMIT DLEERLRREE KQRQELEKTR RKLEGDSTDL SDQIAELQAQ IAELKMQLAK 1080
KEEELQAALA RVEEEAAQKN MALKKIRELE TQISELQEDL ESERASRNKA EKQKRDLGEE 1140
LEALKTELED TLDSTAAQQE LRSKREQEVS ILKKTLEDEA KTHEAQIQEM RQKHSQAVEE 1200
LADQLEQTKR VKATLEKAKQ TLENERGELA NEVKALLQGK GDSEHKRKKV EAQLQELQVK 1260
FSEGERVRTE LADKVTKLQV ELDSVTGLLS QSDSKSSKLT KDFSALESQL QDTQELLQEE 1320
NRQKLSLSTK LKQMEDEKNS FREQLEEEEE AKRNLEKQIA TLHAQVTDMK KKMEDGVGCL 1380
ETAEEAKRRL QKDLEGLSQR LEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSVSNLE 1440
KKQKKFDQLL AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK 1500
QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA TEDAKLRLEV 1560
NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED ERKQRSMAMA ARKKLEMDLK 1620
DLEAHIDTAN KNREEAIKQL RKLQAQMKDC MRELDDTRAS REEILAQAKE NEKKLKSMEA 1680
EMIQLQEELA AAERAKRQAQ QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE 1740
EQGNTELIND RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KAKLQEMESA 1800
VKSKYKASIA ALEAKIAQLE EQLDNETKER QAASKQVRRT EKKLKDVLLQ VEDERRNAEQ 1860
FKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL EDATETADAM NREVSSLKNK 1920
LRRGDLPFVV TRRIVRKGTG DCSDEEVDGK ADGADAKAAE 1960 
Gene Ontology
 GO:0005826; C:actomyosin contractile ring; ISS:UniProtKB.
 GO:0005913; C:cell-cell adherens junction; IDA:MGI.
 GO:0032154; C:cleavage furrow; ISS:UniProtKB.
 GO:0030863; C:cortical cytoskeleton; IDA:MGI.
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0008305; C:integrin complex; IEA:Compara.
 GO:0016460; C:myosin II complex; IDA:MGI.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0005886; C:plasma membrane; ISS:UniProtKB.
 GO:0001726; C:ruffle; ISS:UniProtKB.
 GO:0008180; C:signalosome; IEA:Compara.
 GO:0001725; C:stress fiber; ISS:UniProtKB.
 GO:0001931; C:uropod; IDA:MGI.
 GO:0051015; F:actin filament binding; ISS:UniProtKB.
 GO:0030898; F:actin-dependent ATPase activity; IEA:Compara.
 GO:0043531; F:ADP binding; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; ISS:UniProtKB.
 GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
 GO:0043495; F:protein anchor; ISS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
 GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
 GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
 GO:0001525; P:angiogenesis; ISS:UniProtKB.
 GO:0043534; P:blood vessel endothelial cell migration; ISS:UniProtKB.
 GO:0016337; P:cell-cell adhesion; IMP:MGI.
 GO:0000910; P:cytokinesis; ISS:UniProtKB.
 GO:0051295; P:establishment of meiotic spindle localization; IDA:MGI.
 GO:0001768; P:establishment of T cell polarity; IMP:MGI.
 GO:0001701; P:in utero embryonic development; IMP:MGI.
 GO:0000212; P:meiotic spindle organization; IDA:MGI.
 GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
 GO:0030224; P:monocyte differentiation; ISS:UniProtKB.
 GO:0007520; P:myoblast fusion; IMP:MGI.
 GO:0030220; P:platelet formation; ISS:UniProtKB.
 GO:0015031; P:protein transport; ISS:UniProtKB.
 GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
 GO:0032796; P:uropod organization; IMP:MGI. 
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
 PF00612; IQ
 PF00063; Myosin_head
 PF02736; Myosin_N
 PF01576; Myosin_tail_1 
SMART
 SM00015; IQ
 SM00242; MYSc 
PROSITE
 PS50096; IQ 
PRINTS
 PR00193; MYOSINHEAVY.