CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006505
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myosin-10 
Protein Synonyms/Alias
 Cellular myosin heavy chain, type B; Myosin heavy chain 10; Myosin heavy chain, non-muscle IIb; Non-muscle myosin heavy chain B; NMMHC-B; Non-muscle myosin heavy chain IIb; NMMHC II-b; NMMHC-IIB 
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
51GFEAASIKEERGDEVubiquitination[1]
232LESFGNAKTVKNDNSubiquitination[1, 2]
410VGRDYVQKAQTKEQAubiquitination[1]
442WLVHRINKALDRTKRacetylation[3]
552TDKTFVEKLVQEQGSacetylation[3]
644TAFGSAYKTKKGMFRubiquitination[1]
767LYRIGQSKIFFRAGVubiquitination[2]
817QQQLSALKVLQRNCAubiquitination[2]
840QWWRVFTKVKPLLQVubiquitination[2]
1247VKVLQQVKAESEHKRacetylation[3]
1645KARDEVIKQLRKLQAacetylation[3]
1800QNKELKAKLQELEGAubiquitination[2]
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] 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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. 
Sequence Annotation
 DOMAIN 2 785 Myosin head-like.
 DOMAIN 786 815 IQ.
 NP_BIND 178 185 ATP (Potential).
 MOD_RES 442 442 N6-acetyllysine.
 MOD_RES 1145 1145 Phosphoserine.
 MOD_RES 1645 1645 N6-acetyllysine.
 MOD_RES 1938 1938 Phosphoserine.
 MOD_RES 1939 1939 Phosphoserine.
 MOD_RES 1952 1952 Phosphoserine.
 MOD_RES 1956 1956 Phosphoserine.  
Keyword
 Acetylation; Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding; Cell shape; Coiled coil; Complete proteome; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1976 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 PGELERQLLQ ANPILESFGN AKTVKNDNSS 240
RFGKFIRINF DVTGYIVGAN IETYLLEKSR AVRQAKDERT FHIFYQLLSG AGEHLKSDLL 300
LEGFNNYRFL SNGYIPIPGQ QDKDNFQETM EAMHIMGFSH EEILSMLKVV SSVLQFGNIS 360
FKKERNTDQA SMPENTVAQK LCHLLGMNVM EFTRAILTPR IKVGRDYVQK AQTKEQADFA 420
VEALAKATYE RLFRWLVHRI NKALDRTKRQ GASFIGILDI AGFEIFELNS FEQLCINYTN 480
EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCID LIERPANPPG VLALLDEECW 540
FPKATDKTFV EKLVQEQGSH SKFQKPRQLK DKADFCIIHY AGKVDYKADE WLMKNMDPLN 600
DNVATLLHQS SDRFVAELWK DVDRIVGLDQ VTGMTETAFG SAYKTKKGMF RTVGQLYKES 660
LTKLMATLRN TNPNFVRCII PNHEKRAGKL DPHLVLDQLR CNGVLEGIRI CRQGFPNRIV 720
FQEFRQRYEI LTPNAIPKGF MDGKQACERM IRALELDPNL YRIGQSKIFF RAGVLAHLEE 780
ERDLKITDII IFFQAVCRGY LARKAFAKKQ QQLSALKVLQ RNCAAYLKLR HWQWWRVFTK 840
VKPLLQVTRQ EEELQAKDEE LLKVKEKQTK VEGELEEMER KHQQLLEEKN ILAEQLQAET 900
ELFAEAEEMR ARLAAKKQEL EEILHDLESR VEEEEERNQI LQNEKKKMQA HIQDLEEQLD 960
EEEGARQKLQ LEKVTAEAKI KKMEEEILLL EDQNSKFIKE KKLMEDRIAE CSSQLAEEEE 1020
KAKNLAKIRN KQEVMISDLE ERLKKEEKTR QELEKAKRKL DGETTDLQDQ IAELQAQIDE 1080
LKLQLAKKEE ELQGALARGD DETLHKNNAL KVVRELQAQI AELQEDFESE KASRNKAEKQ 1140
KRDLSEELEA LKTELEDTLD TTAAQQELRT KREQEVAELK KALEEETKNH EAQIQDMRQR 1200
HATALEELSE QLEQAKRFKA NLEKNKQGLE TDNKELACEV KVLQQVKAES EHKRKKLDAQ 1260
VQELHAKVSE GDRLRVELAE KASKLQNELD NVSTLLEEAE KKGIKFAKDA ASLESQLQDT 1320
QELLQEETRQ KLNLSSRIRQ LEEEKNSLQE QQEEEEEARK NLEKQVLALQ SQLADTKKKV 1380
DDDLGTIESL EEAKKKLLKD AEALSQRLEE KALAYDKLEK TKNRLQQELD DLTVDLDHQR 1440
QVASNLEKKQ KKFDQLLAEE KSISARYAEE RDRAEAEARE KETKALSLAR ALEEALEAKE 1500
EFERQNKQLR ADMEDLMSSK DDVGKNVHEL EKSKRALEQQ VEEMRTQLEE LEDELQATED 1560
AKLRLEVNMQ AMKAQFERDL QTRDEQNEEK KRLLIKQVRE LEAELEDERK QRALAVASKK 1620
KMEIDLKDLE AQIEAANKAR DEVIKQLRKL QAQMKDYQRE LEEARASRDE IFAQSKESEK 1680
KLKSLEAEIL QLQEELASSE RARRHAEQER DELADEITNS ASGKSALLDE KRRLEARIAQ 1740
LEEELEEEQS NMELLNDRFR KTTLQVDTLN AELAAERSAA QKSDNARQQL ERQNKELKAK 1800
LQELEGAVKS KFKATISALE AKIGQLEEQL EQEAKERAAA NKLVRRTEKK LKEIFMQVED 1860
ERRHADQYKE QMEKANARMK QLKRQLEEAE EEATRANASR RKLQRELDDA TEANEGLSRE 1920
VSTLKNRLRR GGPISFSSSR SGRRQLHLEG ASLELSDDDT ESKTSDVNET QPPQSE 1976 
Gene Ontology
 GO:0005938; C:cell cortex; IDA:UniProtKB.
 GO:0032154; C:cleavage furrow; IDA:UniProtKB.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0016459; C:myosin complex; NAS:UniProtKB.
 GO:0001725; C:stress fiber; IDA:UniProtKB.
 GO:0051015; F:actin filament binding; IDA:MGI.
 GO:0030898; F:actin-dependent ATPase activity; IDA:MGI.
 GO:0043531; F:ADP binding; IDA:MGI.
 GO:0005524; F:ATP binding; NAS:UniProtKB.
 GO:0000146; F:microfilament motor activity; IDA:MGI.
 GO:0030048; P:actin filament-based movement; IDA:MGI.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0000281; P:mitotic cytokinesis; IDA:MGI.
 GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 
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.