UniProt Accession

 MYH9_HUMAN; P35579; O60805; Q86T83 

Genbank Protein ID

 CR456526; AL832639; Z82215; M81105; M69180; M31013 

Genbank Nucleotide ID

 CAG30412.1; CAD89954.1; CAB05105.1; AAA59888.1; AAA61765.1; AAA36349.1 

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

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
8	MAQQAADKYLYVDKN	acetylation	[1]
8	MAQQAADKYLYVDKN	ubiquitination	[2, 3, 4, 5]
14	DKYLYVDKNFINNPL	ubiquitination	[2, 3, 4, 5, 6]
29	AQADWAAKKLVWVPS	ubiquitination	[4, 6, 7]
30	QADWAAKKLVWVPSD	ubiquitination	[4]
38	LVWVPSDKSGFEPAS	ubiquitination	[2, 3, 5]
64	ELVENGKKVKVNKDD	ubiquitination	[4]
66	VENGKKVKVNKDDIQ	ubiquitination	[4]
69	GKKVKVNKDDIQKMN	ubiquitination	[6]
74	VNKDDIQKMNPPKFS	acetylation	[1]
79	IQKMNPPKFSKVEDM	ubiquitination	[3]
82	MNPPKFSKVEDMAEL	ubiquitination	[4]
102	ASVLHNLKERYYSGL	acetylation	[1]
102	ASVLHNLKERYYSGL	ubiquitination	[4, 8]
141	IVEMYKGKKRHEMPP	ubiquitination	[4]
186	GKTENTKKVIQYLAY	acetylation	[9]
186	GKTENTKKVIQYLAY	ubiquitination	[3, 4]
201	VASSHKSKKDQGELE	ubiquitination	[4]
225	LEAFGNAKTVKNDNS	ubiquitination	[2, 3, 4, 5, 6, 7, 10]
237	DNSSRFGKFIRINFD	ubiquitination	[4]
289	SGAGEHLKTDLLLEP	acetylation	[9]
299	LLLEPYNKYRFLSNG	acetylation	[1, 8, 11, 12]
299	LLLEPYNKYRFLSNG	ubiquitination	[2, 3, 4, 5, 6, 7, 8]
355	QLGNIVFKKERNTDQ	acetylation	[8]
356	LGNIVFKKERNTDQA	ubiquitination	[4]
373	PDNTAAQKVSHLLGI	ubiquitination	[2, 4, 5, 6, 8, 13]
403	VGRDYVQKAQTKEQA	ubiquitination	[4, 7]
540	WFPKATDKSFVEKVM	ubiquitination	[4]
545	TDKSFVEKVMQEQGT	acetylation	[1, 8, 11, 12]
545	TDKSFVEKVMQEQGT	ubiquitination	[3, 4, 6, 8]
555	QEQGTHPKFQKPKQL	acetylation	[12]
565	KPKQLKDKADFCIIH	ubiquitination	[3]
580	YAGKVDYKADEWLMK	ubiquitination	[3]
613	KFVSELWKDVDRIIG	acetylation	[11]
637	TALPGAFKTRKGMFR	ubiquitination	[2, 3, 4, 5, 6, 7, 8, 13]
640	PGAFKTRKGMFRTVG	ubiquitination	[4]
651	RTVGQLYKEQLAKLM	acetylation	[11, 12]
651	RTVGQLYKEQLAKLM	ubiquitination	[2, 3, 4, 5, 8, 10]
679	IIPNHEKKAGKLDPH	ubiquitination	[4, 8]
682	NHEKKAGKLDPHLVL	ubiquitination	[2, 3, 4, 5, 6, 7, 10]
731	LTPNSIPKGFMDGKQ	ubiquitination	[3]
760	LYRIGQSKVFFRAGV	ubiquitination	[2, 3, 4, 5, 7, 8, 10]
810	QQQLTAMKVLQRNCA	ubiquitination	[2, 3, 5]
821	RNCAAYLKLRNWQWW	acetylation	[1]
821	RNCAAYLKLRNWQWW	ubiquitination	[4, 7, 10, 13]
833	QWWRLFTKVKPLLQV	ubiquitination	[2, 3, 4, 5]
835	WRLFTKVKPLLQVSR	acetylation	[14]
835	WRLFTKVKPLLQVSR	ubiquitination	[2, 3, 4, 5]
860	ELVKVREKQLAAENR	ubiquitination	[3, 6, 7]
974	VTTEAKLKKLEEEQI	ubiquitination	[6]
975	TTEAKLKKLEEEQII	ubiquitination	[4, 6]
1014	NLTEEEEKSKSLAKL	acetylation	[12]
1024	SLAKLKNKHEAMITD	acetylation	[1, 8, 9, 11, 12]
1048	KQRQELEKTRRKLEG	acetylation	[8]
1234	GELANEVKVLLQGKG	acetylation	[12]
1234	GELANEVKVLLQGKG	ubiquitination	[2, 3, 5]
1248	GDSEHKRKKVEAQLQ	acetylation	[8]
1248	GDSEHKRKKVEAQLQ	ubiquitination	[4, 8]
1249	DSEHKRKKVEAQLQE	acetylation	[8]
1249	DSEHKRKKVEAQLQE	ubiquitination	[4, 8]
1260	QLQELQVKFNEGERV	acetylation	[9]
1260	QLQELQVKFNEGERV	ubiquitination	[6]
1274	VRTELADKVTKLQVE	acetylation	[1]
1274	VRTELADKVTKLQVE	ubiquitination	[3, 4, 6, 7, 8]
1277	ELADKVTKLQVELDN	ubiquitination	[8]
1301	SKSSKLTKDFSALES	acetylation	[12]
1301	SKSSKLTKDFSALES	ubiquitination	[4, 6, 7]
1330	QKLSLSTKLKQVEDE	ubiquitination	[4]
1352	LEEEEEAKHNLEKQI	acetylation	[8, 9, 12]
1357	EAKHNLEKQIATLHA	acetylation	[1, 11, 12]
1357	EAKHNLEKQIATLHA	ubiquitination	[6]
1370	HAQVADMKKKMEDSV	ubiquitination	[6]
1392	EVKRKLQKDLEGLSQ	acetylation	[1, 8, 11, 12]
1392	EVKRKLQKDLEGLSQ	ubiquitination	[2, 3, 4, 5]
1404	LSQRHEEKVAAYDKL	acetylation	[1, 8, 11]
1410	EKVAAYDKLEKTKTR	acetylation	[1, 8, 11]
1413	AAYDKLEKTKTRLQQ	ubiquitination	[4, 7, 8]
1415	YDKLEKTKTRLQQEL	ubiquitination	[4, 8]
1441	QSACNLEKKQKKFDQ	acetylation	[1, 8, 12]
1445	NLEKKQKKFDQLLAE	ubiquitination	[2, 3, 4, 5]
1454	DQLLAEEKTISAKYA	acetylation	[8, 11]
1459	EEKTISAKYAEERDR	acetylation	[1, 8, 11]
1459	EEKTISAKYAEERDR	ubiquitination	[3]
1477	EAREKETKALSLARA	ubiquitination	[3]
1492	LEEAMEQKAELERLN	acetylation	[11, 12]
1513	MEDLMSSKDDVGKSV	acetylation	[12]
1525	KSVHELEKSKRALEQ	acetylation	[8, 11, 12]
1566	EVNLQAMKAQFERDL	ubiquitination	[2, 3, 4, 5]
1613	SMAVAARKKLEMDLK	ubiquitination	[4]
1638	KNRDEAIKQLRKLQA	acetylation	[1, 8, 11]
1669	EEILAQAKENEKKLK	ubiquitination	[6]
1676	KENEKKLKSMEAEMI	ubiquitination	[6]
1696	LAAAERAKRQAQQER	ubiquitination	[6]
1724	GALALEEKRRLEARI	acetylation	[8]
1754	LINDRLKKANLQIDQ	ubiquitination	[3]
1793	QNKELKVKLQEMEGT	acetylation	[8, 12]
1793	QNKELKVKLQEMEGT	ubiquitination	[6]
1802	QEMEGTVKSKYKASI	acetylation	[11]
1804	MEGTVKSKYKASITA	ubiquitination	[7]
1806	GTVKSKYKASITALE	ubiquitination	[7]
1828	EQLDNETKERQAACK	acetylation	[8, 12]
1845	RRTEKKLKDVLLQVD	acetylation	[8]
1862	RRNAEQYKDQADKAS	acetylation	[8]
1867	QYKDQADKASTRLKQ	acetylation	[8]

Reference

 [1] 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]
 [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] 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]
 [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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [14] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330] 

Functional Description

 Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. 

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.
 MOD_RES 11 11 Phosphotyrosine.
 MOD_RES 102 102 N6-acetyllysine.
 MOD_RES 181 181 Phosphothreonine (By similarity).
 MOD_RES 299 299 N6-acetyllysine.
 MOD_RES 754 754 Phosphotyrosine (By similarity).
 MOD_RES 1024 1024 N6-acetyllysine.
 MOD_RES 1357 1357 N6-acetyllysine.
 MOD_RES 1392 1392 N6-acetyllysine.
 MOD_RES 1404 1404 N6-acetyllysine.
 MOD_RES 1410 1410 N6-acetyllysine.
 MOD_RES 1459 1459 N6-acetyllysine.
 MOD_RES 1638 1638 N6-acetyllysine.
 MOD_RES 1714 1714 Phosphoserine.
 MOD_RES 1943 1943 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Actin-binding; Alport syndrome; Alternative splicing; ATP-binding; Calmodulin-binding; Cataract; Cell shape; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Deafness; Direct protein sequencing; Disease mutation; Motor protein; Myosin; Non-syndromic deafness; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1960 AA 

Protein Sequence

Gene Ontology

 GO:0005826; C:actomyosin contractile ring; IDA:UniProtKB.
 GO:0005913; C:cell-cell adherens junction; IEA:Compara.
 GO:0032154; C:cleavage furrow; IDA:UniProtKB.
 GO:0030863; C:cortical cytoskeleton; IEA:Compara.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0001772; C:immunological synapse; IEA:Compara.
 GO:0016460; C:myosin II complex; IEA:Compara.
 GO:0031594; C:neuromuscular junction; IEA:Compara.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0043234; C:protein complex; IDA:UniProtKB.
 GO:0001726; C:ruffle; IDA:UniProtKB.
 GO:0005819; C:spindle; IEA:Compara.
 GO:0001725; C:stress fiber; IDA:UniProtKB.
 GO:0001931; C:uropod; IDA:MGI.
 GO:0051015; F:actin filament binding; IDA:UniProtKB.
 GO:0030898; F:actin-dependent ATPase activity; IDA:MGI.
 GO:0043531; F:ADP binding; IDA:MGI.
 GO:0005524; F:ATP binding; IDA:MGI.
 GO:0000146; F:microfilament motor activity; IDA:UniProtKB.
 GO:0043495; F:protein anchor; IMP:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
 GO:0030048; P:actin filament-based movement; IDA:UniProtKB.
 GO:0001525; P:angiogenesis; IDA:UniProtKB.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0043534; P:blood vessel endothelial cell migration; IMP:UniProtKB.
 GO:0016337; P:cell-cell adhesion; IEA:Compara.
 GO:0000910; P:cytokinesis; IMP:UniProtKB.
 GO:0051295; P:establishment of meiotic spindle localization; IEA:Compara.
 GO:0001768; P:establishment of T cell polarity; IEA:Compara.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
 GO:0050900; P:leukocyte migration; NAS:UniProtKB.
 GO:0000212; P:meiotic spindle organization; IEA:Compara.
 GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
 GO:0030224; P:monocyte differentiation; IEP:UniProtKB.
 GO:0007520; P:myoblast fusion; IEA:Compara.
 GO:0030220; P:platelet formation; IMP:UniProtKB.
 GO:0015031; P:protein transport; IMP:UniProtKB.
 GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
 GO:0038032; P:termination of G-protein coupled receptor signaling pathway; IEA:InterPro.
 GO:0032796; P:uropod organization; IEA:Compara. 

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.
 IPR016137; Regulat_G_prot_signal_superfam. 

Pfam

 PF00612; IQ
 PF00063; Myosin_head
 PF02736; Myosin_N
 PF01576; Myosin_tail_1 

SMART

 SM00015; IQ
 SM00242; MYSc 

PROSITE

 PS50096; IQ 

PRINTS

 PR00193; MYOSINHEAVY.