CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006506
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
83IQKMNPPKFSKVEDMubiquitination[1]
232LESFGNAKTVKNDNSubiquitination[1]
572KPRQLKDKADFCIIHubiquitination[1]
587YAGKVDYKADEWLMKubiquitination[1]
710NHEKRAGKLDPHLVLubiquitination[1]
788LYRIGQSKIFFRAGVubiquitination[1]
838QQQLSALKVLQRNCAubiquitination[1]
1473NLEKKQKKFDQLLAEubiquitination[1]
1505EAREKETKALSLARAubiquitination[1]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
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 DEIQNIQRAS FYDSVSGLHE PPVDRIVGLD QVTGMTETAF 660
GSAYKTKKGM FRTVGQLYKE SLTKLMATLR NTNPNFVRCI IPNHEKRAGK LDPHLVLDQL 720
RCNGVLEGIR ICRQGFPNRI VFQEFRQRYE ILTPNAIPKG FMDGKQACER MIRALELDPN 780
LYRIGQSKIF FRAGVLAHLE EERDLKITDI IIFFQAVCRG YLARKAFAKK QQQLSALKVL 840
QRNCAAYLKL RHWQWWRVFT KVKPLLQVTR QEEELQAKDE ELLKVKEKQT KVEGELEEME 900
RKHQQLLEEK NILAEQLQAE TELFAEAEEM RARLAAKKQE LEEILHDLES RVEEEEERNQ 960
ILQNEKKKMQ AHIQDLEEQL DEEEGARQKL QLEKVTAEAK IKKMEEEILL LEDQNSKFIK 1020
EKKLMEDRIA ECSSQLAEEE EKAKNLAKIR NKQEVMISDL EERLKKEEKT RQELEKAKRK 1080
LDGETTDLQD QIAELQAQID ELKLQLAKKE EELQGALARG DDETLHKNNA LKVVRELQAQ 1140
IAELQEDFES EKASRNKAEK QKRDLSEELE ALKTELEDTL DTTAAQQELR TKREQEVAEL 1200
KKALEEETKN HEAQIQDMRQ RHATALEELS EQLEQAKRFK ANLEKNKQGL ETDNKELACE 1260
VKVLQQVKAE SEHKRKKLDA QVQELHAKVS EGDRLRVELA EKASKLQNEL DNVSTLLEEA 1320
EKKGIKFAKD AASLESQLQD TQELLQEETR QKLNLSSRIR QLEEEKNSLQ EQQEEEEEAR 1380
KNLEKQVLAL QSQLADTKKK VDDDLGTIES LEEAKKKLLK DAEALSQRLE EKALAYDKLE 1440
KTKNRLQQEL DDLTVDLDHQ RQVASNLEKK QKKFDQLLAE EKSISARYAE ERDRAEAEAR 1500
EKETKALSLA RALEEALEAK EEFERQNKQL RADMEDLMSS KDDVGKNVHE LEKSKRALEQ 1560
QVEEMRTQLE ELEDELQATE DAKLRLEVNM QAMKAQFERD LQTRDEQNEE KKRLLIKQVR 1620
ELEAELEDER KQRALAVASK KKMEIDLKDL EAQIEAANKA RDEVIKQLRK LQAQMKDYQR 1680
ELEEARASRD EIFAQSKESE KKLKSLEAEI LQLQEELASS ERARRHAEQE RDELADEITN 1740
SASGKSALLD EKRRLEARIA QLEEELEEEQ SNMELLNDRF RKTTLQVDTL NAELAAERSA 1800
AQKSDNARQQ LERQNKELKA KLQELEGAVK SKFKATISAL EAKIGQLEEQ LEQEAKERAA 1860
ANKLVRRTEK KLKEIFMQVE DERRHADQYK EQMEKANARM KQLKRQLEEA EEEATRANAS 1920
RRKLQRELDD ATEANEGLSR EVSTLKNRLR RGGPISFSSS RSGRRQLHLE GASLELSDDD 1980
TESKTSDVNE TQPPQSE 1997 
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.