Reviewed, UniProtKB/Swiss-Prot P35579 (MYH9_HUMAN)

Names and origin

Protein names

Recommended name:
    Myosin-9
Alternative name(s):
    Myosin heavy chain 9
    Myosin heavy chain, non-muscle IIa
    Non-muscle myosin heavy chain IIa
      Short name=NMMHC II-a
      Short name=NMMHC-IIA
    Cellular myosin heavy chain, type A
    Non-muscle myosin heavy chain A
      Short name=NMMHC-A

Gene names

Name:

MYH9

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1960 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping.
Subunit structure	Interacts with PDLIM2 By similarity. Myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2).
Tissue specificity	In the kidney, expressed in the glomeruli. Also expressed in leukocytes. Ref.4 Ref.25
Domain	The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.
Involvement in disease	Defects in MYH9 are the cause of May-Hegglin anomaly (MHA) [MIM:155100]. MHA is an autosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukokyte inclusions appearing as highly parallel paracrystalline bodies. Ref.20 Ref.21 Ref.22 Ref.23 Ref.27 Ref.28 Ref.32 Defects in MYH9 are the cause of Sebastian syndrome (SBS) [MIM:605249]. SBS is an autosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukocyte inclusions that are smaller and less organized than in May-Hegglin anomaly. Ref.27 Ref.32 Defects in MYH9 are the cause of Fechtner syndrome (FTNS) [MIM:153640]. FTNS is an autosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukocyte inclusions that are small and poorly organized. Additionally, FTNS is distinguished by Alport-like clinical features of sensorineural deafness, cataracts and nephritis. Ref.25 Ref.27 Ref.28 Ref.32 Defects in MYH9 are the cause of Alport syndrome with macrothrombocytopenia (APSM) [MIM:153650]. APSM is an autosomal dominant disorder characterized by the association of ocular lesions, sensorineural hearing loss and nephritis (Alport syndrome) with platelet defects. Ref.32 Defects in MYH9 are the cause of Epstein syndrome (EPS) [MIM:153650]. EPS is an autosomal dominant disorder characterized by the association of macrothrombocytopathy, sensorineural hearing loss and nephritis. Ref.27 Ref.28 Ref.32 Ref.24 Ref.30 Defects in MYH9 are the cause of non-syndromic sensorineural deafness autosomal dominant type 17 (DFNA17) [MIM:603622]. DFNA17 is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA17 is characterized by progressive hearing impairment and cochleosaccular degeneration. Ref.32 Ref.19 Defects in MYH9 are the cause of macrothrombocytopenia with progressive sensorineural deafness (MPSD) [MIM:600208]. MPSD is an autosomal dominant disorder characterized by the association of macrothrombocytopathy and progressive sensorineural hearing loss without renal dysfunction. Ref.32 Ref.29 Subjects with mutations in the motor domain of MYH9 present with severe thrombocytopenia and develop nephritis and deafness before the age of 40 years, while those with mutations in the tail domain have a much lower risk of noncongenital complications and significantly higher platelet counts. The clinical course of patients with mutations in the four most frequently affected residues of MYH9 (responsible for 70% of MYH9-related cases) were evaluated. Mutations at residue 1933 do not induce kidney damage or cataracts and cause deafness only in the elderly, those in position 702 result in severe thrombocytopenia and produce nephritis and deafness at a juvenile age, while alterations at residue 1424 or 1841 result in intermediate clinical pictures. Ref.32
Sequence similarities	Contains 1 IQ domain. Contains 1 myosin head-like domain.
Sequence caution	The sequence CAD89954.1 differs from that shown. Reason: Frameshift at position 1890.

Ontologies

Keywords
Biological process	Cell shape
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Alport syndrome Cataract Deafness Disease mutation Non-syndromic deafness
Domain	Coiled coil
Ligand	ATP-binding Actin-binding Calmodulin-binding Nucleotide-binding
Molecular function	Motor protein Myosin
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	actin cytoskeleton reorganization Inferred from mutant phenotype. Source: UniProtKB actin filament-based movement Inferred from direct assay. Source: UniProtKB angiogenesis Inferred from direct assay. Source: UniProtKB blood vessel endothelial cell migration Inferred from mutant phenotype. Source: UniProtKB cytokinesis Inferred from mutant phenotype. Source: UniProtKB integrin-mediated signaling pathway Non-traceable author statement. Source: UniProtKB leukocyte migration Non-traceable author statement. Source: UniProtKB membrane protein ectodomain proteolysis Inferred from direct assay. Source: UniProtKB monocyte differentiation Ref.4 Inferred from expression pattern. Source: UniProtKB platelet formation Inferred from mutant phenotype. Source: UniProtKB protein transport Inferred from mutant phenotype. Source: UniProtKB regulation of cell shape Inferred from mutant phenotype. Source: UniProtKB sensory perception of sound Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cleavage furrow Inferred from direct assay. Source: UniProtKB contractile ring Inferred from direct assay. Source: UniProtKB cytosol Inferred from direct assay. Source: UniProtKB myosin complex Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: UniProtKB ruffle Inferred from direct assay. Source: UniProtKB stress fiber Inferred from direct assay. Source: UniProtKB uropod Inferred from direct assay. Source: MGI
Molecular function	ADP binding Inferred from direct assay. Source: MGI ATP binding Inferred from direct assay. Source: MGI actin filament binding Inferred from direct assay. Source: UniProtKB actin-dependent ATPase activity Inferred from direct assay. Source: MGI calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW microfilament motor activity Inferred from direct assay. Source: UniProtKB protein anchor Inferred from mutant phenotype. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCR5	P51681	1	EBI-350338,EBI-489374
CXCR4	P61073	4	EBI-350338,EBI-489411
EPB41	P11171	1	EBI-350338,EBI-1050906
MEN1	O00255	5	EBI-350338,EBI-592789
NCL	P19338	2	EBI-350338,EBI-352553
S100P	P25815	1	EBI-350338,EBI-743700

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P35579-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P35579-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-136: Missing.
     980-1421: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 1960	1959	Myosin-9		PRO_0000123416
Regions
	Domain	2 – 778	777	Myosin head-like
	Domain	779 – 808	30	IQ
	Nucleotide binding	174 – 181	8	ATP Potential
	Region	654 – 676	23	Actin-binding
	Coiled coil	837 – 1926	1090	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.6
	Modified residue	181	1	Phosphothreonine By similarity
	Modified residue	638	1	Phosphothreonine By similarity
	Modified residue	754	1	Phosphotyrosine Ref.12
	Modified residue	1408	1	Phosphotyrosine Ref.12
	Modified residue	1714	1	Phosphoserine Ref.15
	Modified residue	1943	1	Phosphoserine Ref.15 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17
Natural variations
	Alternative sequence	1 – 136	136	Missing in isoform 2.		VSP_035409
	Alternative sequence	980 – 1421	442	Missing in isoform 2.		VSP_035410
	Natural variant	93	1	N → K in MHA. Ref.20		VAR_010791
	Natural variant	95	1	A → T in MHA. Ref.23		VAR_018308
	Natural variant	96	1	S → L in EPS. Ref.30		VAR_018309
	Natural variant	373	1	K → N in MHA and SBS.		VAR_018310
	Natural variant	702	1	R → C in APSM, EPS, FTNS, MHA and SBS.		VAR_010792
	Natural variant	702	1	R → H in APSM and EPS.		VAR_018311
	Natural variant	705	1	R → H in DFNA17. Ref.19		VAR_010793
	Natural variant	810	1	K → N in a breast cancer sample; somatic mutation. Ref.31		VAR_036006
	Natural variant	910	1	K → Q in FTNS. Ref.28		VAR_044226
	Natural variant	967	1	V → E: dbSNP rs16996652.		VAR_044227
	Natural variant	1066 – 1072	7	Missing in MHA and SBS.		VAR_044228
	Natural variant	1114	1	S → P in APSM.		VAR_018312
	Natural variant	1155	1	T → I in MHA and FTNS.		VAR_010794
	Natural variant	1165	1	R → C in FTNS and SBS.		VAR_010795
	Natural variant	1165	1	R → L in FTNS, MHA and SBS.		VAR_018313
	Natural variant	1205 – 1207	3	Missing in SBS. Ref.27		VAR_018314
	Natural variant	1400	1	R → W in a EPS patient; might contribute to pathogenicity; when associated with L-96. Ref.25		VAR_018315
	Natural variant	1424	1	D → H in FTNS and MHA.		VAR_010796
	Natural variant	1424	1	D → N in FTNS, MHA, SBS and MPSD; affects protein stability.		VAR_018316
	Natural variant	1424	1	D → Y in MHA. Ref.20 Ref.22 Ref.23 Ref.27 Ref.28		VAR_018317
	Natural variant	1626	1	I → V: dbSNP rs2269529. Ref.23		VAR_018318
	Natural variant	1816	1	I → V in EPS. Ref.27		VAR_030385
	Natural variant	1841	1	E → K in FTNS, SBS, MHA and EPS.		VAR_010797
Experimental info
	Sequence conflict	53 – 55	3	EAI → RGH Ref.5
	Sequence conflict	660	1	T → S Ref.5
	Sequence conflict	869	1	T → M in AAA36349. Ref.7
	Sequence conflict	931	1	C → Y in AAA36349. Ref.7
	Sequence conflict	1240 – 1241	2	KG → GR in AAA36349. Ref.7
	Sequence conflict	1350	1	E → EE Ref.7
	Sequence conflict	1462	1	E → G in CAD89954. Ref.1
	Sequence conflict	1546	1	D → G in CAD89954. Ref.1
	Sequence conflict	1764	1	T → A in AAA36349. Ref.7
	Sequence conflict	1771	1	S → G in AAA36349. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 588F84BB8C106E6F	FASTA	1,960	226,532
	10 20 30 40 50 60 MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSDKSG FEPASLKEEV GEEAIVELVE 70 80 90 100 110 120 NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN LKERYYSGLI YTYSGLFCVV 130 140 150 160 170 180 INPYKNLPIY SEEIVEMYKG KKRHEMPPHI YAITDTAYRS MMQDREDQSI LCTGESGAGK 190 200 210 220 230 240 TENTKKVIQY LAYVASSHKS KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR 250 260 270 280 290 300 INFDVNGYIV GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY 310 320 330 340 350 360 RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEEEQMGLL RVISGVLQLG NIVFKKERNT 370 380 390 400 410 420 DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY VQKAQTKEQA DFAIEALAKA 430 440 450 460 470 480 TYERMFRWLV LRINKALDKT KRQGASFIGI LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF 490 500 510 520 530 540 NHTMFILEQE EYQREGIEWN FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK 550 560 570 580 590 600 SFVEKVMQEQ GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL 610 620 630 640 650 660 HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY KEQLAKLMAT 670 680 690 700 710 720 LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG IRICRQGFPN RVVFQEFRQR 730 740 750 760 770 780 YEILTPNSIP KGFMDGKQAC VLMIKALELD SNLYRIGQSK VFFRAGVLAH LEEERDLKIT 790 800 810 820 830 840 DVIIGFQACC RGYLARKAFA KRQQQLTAMK VLQRNCAAYL KLRNWQWWRL FTKVKPLLQV 850 860 870 880 890 900 SRQEEEMMAK EEELVKVREK QLAAENRLTE METLQSQLMA EKLQLQEQLQ AETELCAEAE 910 920 930 940 950 960 ELRARLTAKK QELEEICHDL EARVEEEEER CQHLQAEKKK MQQNIQELEE QLEEEESARQ 970 980 990 1000 1010 1020 KLQLEKVTTE AKLKKLEEEQ IILEDQNCKL AKEKKLLEDR IAEFTTNLTE EEEKSKSLAK 1030 1040 1050 1060 1070 1080 LKNKHEAMIT DLEERLRREE KQRQELEKTR RKLEGDSTDL SDQIAELQAQ IAELKMQLAK 1090 1100 1110 1120 1130 1140 KEEELQAALA RVEEEAAQKN MALKKIRELE SQISELQEDL ESERASRNKA EKQKRDLGEE 1150 1160 1170 1180 1190 1200 LEALKTELED TLDSTAAQQE LRSKREQEVN ILKKTLEEEA KTHEAQIQEM RQKHSQAVEE 1210 1220 1230 1240 1250 1260 LAEQLEQTKR VKANLEKAKQ TLENERGELA NEVKVLLQGK GDSEHKRKKV EAQLQELQVK 1270 1280 1290 1300 1310 1320 FNEGERVRTE LADKVTKLQV ELDNVTGLLS QSDSKSSKLT KDFSALESQL QDTQELLQEE 1330 1340 1350 1360 1370 1380 NRQKLSLSTK LKQVEDEKNS FREQLEEEEE AKHNLEKQIA TLHAQVADMK KKMEDSVGCL 1390 1400 1410 1420 1430 1440 ETAEEVKRKL QKDLEGLSQR HEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSACNLE 1450 1460 1470 1480 1490 1500 KKQKKFDQLL AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK 1510 1520 1530 1540 1550 1560 QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA TEDAKLRLEV 1570 1580 1590 1600 1610 1620 NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED ERKQRSMAVA ARKKLEMDLK 1630 1640 1650 1660 1670 1680 DLEAHIDSAN KNRDEAIKQL RKLQAQMKDC MRELDDTRAS REEILAQAKE NEKKLKSMEA 1690 1700 1710 1720 1730 1740 EMIQLQEELA AAERAKRQAQ QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE 1750 1760 1770 1780 1790 1800 EQGNTELIND RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KVKLQEMEGT 1810 1820 1830 1840 1850 1860 VKSKYKASIT ALEAKIAQLE EQLDNETKER QAACKQVRRT EKKLKDVLLQ VDDERRNAEQ 1870 1880 1890 1900 1910 1920 YKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL EDATETADAM NREVSSLKNK 1930 1940 1950 1960 LRRGDLPFVV PRRMARKGAG DGSDEEVDGK ADGAEAKPAE
	Isoform 2. Checksum: 02727B4F964F5839	FASTA	1,382	159,864
	10 20 30 40 50 60 MYKGKKRHEM PPHIYAITDT AYRSMMQDRE DQSILCTGES GAGKTENTKK VIQYLAYVAS 70 80 90 100 110 120 SHKSKKDQGE LERQLLQANP ILEAFGNAKT VKNDNSSRFG KFIRINFDVN GYIVGANIET 130 140 150 160 170 180 YLLEKSRAIR QAKEERTFHI FYYLLSGAGE HLKTDLLLEP YNKYRFLSNG HVTIPGQQDK 190 200 210 220 230 240 DMFQETMEAM RIMGIPEEEQ MGLLRVISGV LQLGNIVFKK ERNTDQASMP DNTAAQKVSH 250 260 270 280 290 300 LLGINVTDFT RGILTPRIKV GRDYVQKAQT KEQADFAIEA LAKATYERMF RWLVLRINKA 310 320 330 340 350 360 LDKTKRQGAS FIGILDIAGF EIFDLNSFEQ LCINYTNEKL QQLFNHTMFI LEQEEYQREG 370 380 390 400 410 420 IEWNFIDFGL DLQPCIDLIE KPAGPPGILA LLDEECWFPK ATDKSFVEKV MQEQGTHPKF 430 440 450 460 470 480 QKPKQLKDKA DFCIIHYAGK VDYKADEWLM KNMDPLNDNI ATLLHQSSDK FVSELWKDVD 490 500 510 520 530 540 RIIGLDQVAG MSETALPGAF KTRKGMFRTV GQLYKEQLAK LMATLRNTNP NFVRCIIPNH 550 560 570 580 590 600 EKKAGKLDPH LVLDQLRCNG VLEGIRICRQ GFPNRVVFQE FRQRYEILTP NSIPKGFMDG 610 620 630 640 650 660 KQACVLMIKA LELDSNLYRI GQSKVFFRAG VLAHLEEERD LKITDVIIGF QACCRGYLAR 670 680 690 700 710 720 KAFAKRQQQL TAMKVLQRNC AAYLKLRNWQ WWRLFTKVKP LLQVSRQEEE MMAKEEELVK 730 740 750 760 770 780 VREKQLAAEN RLTEMETLQS QLMAEKLQLQ EQLQAETELC AEAEELRARL TAKKQELEEI 790 800 810 820 830 840 CHDLEARVEE EEERCQHLQA EKKKMQQNIQ ELEEQLEEEE SARQKLQLEK VTTEAKLKKL 850 860 870 880 890 900 EEELDDLLVD LDHQRQSACN LEKKQKKFDQ LLAEEKTISA KYAEERDRAE AEAREKETKA 910 920 930 940 950 960 LSLARALEEA MEQKAELERL NKQFRTEMED LMSSKDDVGK SVHELEKSKR ALEQQVEEMK 970 980 990 1000 1010 1020 TQLEELEDEL QATEDAKLRL EVNLQAMKAQ FERDLQGRDE QSEEKKKQLV RQVREMEAEL 1030 1040 1050 1060 1070 1080 EDERKQRSMA VAARKKLEMD LKDLEAHIDS ANKNRDEAIK QLRKLQAQMK DCMRELDDTR 1090 1100 1110 1120 1130 1140 ASREEILAQA KENEKKLKSM EAEMIQLQEE LAAAERAKRQ AQQERDELAD EIANSSGKGA 1150 1160 1170 1180 1190 1200 LALEEKRRLE ARIAQLEEEL EEEQGNTELI NDRLKKANLQ IDQINTDLNL ERSHAQKNEN 1210 1220 1230 1240 1250 1260 ARQQLERQNK ELKVKLQEME GTVKSKYKAS ITALEAKIAQ LEEQLDNETK ERQAACKQVR 1270 1280 1290 1300 1310 1320 RTEKKLKDVL LQVDDERRNA EQYKDQADKA STRLKQLKRQ LEEAEEEAQR ANASRRKLQR 1330 1340 1350 1360 1370 1380 ELEDATETAD AMNREVSSLK NKLRRGDLPF VVPRRMARKG AGDGSDEEVD GKADGAEAKP AE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Spinal cord.
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Cellular myosin heavy chain in human leukocytes: isolation of 5' cDNA clones, characterization of the protein, chromosomal localization, and upregulation during myeloid differentiation." Toothaker L.E., Gonzalez D.A., Tung N., Lemons R.S., le Beau M.M., Arnaout M.A., Clayton L.K., Tenen D.G. Blood 78:1826-1833(1991) [PubMed: 1912569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1337, TISSUE SPECIFICITY.
[5]	"Human nonmuscle myosin heavy chains are encoded by two genes located on different chromosomes." Simons M., Wang M., McBride O.W., Kawamoto S., Yamakawa K., Gdula D., Adelstein R.S., Weir L. Circ. Res. 69:530-539(1991) [PubMed: 1860190] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-715.
[6]	Bienvenut W.V., Claeys R. Submitted (AUG-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-47; 67-74; 126-139; 187-199; 203-225; 241-261; 290-299; 328-355; 359-387; 408-419; 476-494; 546-555; 581-613; 618-637; 645-651; 657-670; 683-693; 712-718; 721-731; 746-755; 765-775; 802-810; 824-829; 834-842; 861-867; 924-930; 995-1014; 1042-1048; 1052-1075; 1081-1099; 1136-1162; 1166-1191; 1261-1266; 1278-1295; 1302-1322; 1393-1400; 1405-1413; 1418-1433; 1484-1492; 1504-1513; 1519-1525; 1529-1555; 1558-1566; 1606-1612; 1614-1638; 1642-1648; 1662-1669; 1704-1724; 1794-1802; 1807-1828; 1857-1867; 1899-1912; 1923-1932 AND 1951-1960, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Platelet.
[7]	"Human nonmuscle myosin heavy chain mRNA: generation of diversity through alternative polyadenylylation." Saez C.G., Myers J.C., Shows T.B., Leinwand L.A. Proc. Natl. Acad. Sci. U.S.A. 87:1164-1168(1990) [PubMed: 1967836] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 714-1960.
[8]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY.
[9]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY. Tissue: T-cell.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-754 AND TYR-1408, MASS SPECTROMETRY.
[13]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY.
[14]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY.
[15]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1714 AND SER-1943, MASS SPECTROMETRY. Tissue: Platelet.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY.
[17]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY. Tissue: Liver.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"Human nonsyndromic hereditary deafness DFNA17 is due to a mutation in nonmuscle myosin MYH9." Lalwani A.K., Goldstein J.A., Kelley M.J., Luxford W., Castelein C.M., Mhatre A.N. Am. J. Hum. Genet. 67:1121-1128(2000) [PubMed: 11023810] [Abstract] Cited for: VARIANT DFNA17 HIS-705.
[20]	"Mutations in MYH9 result in the May-Hegglin anomaly, and Fechtner and Sebastian syndromes." Seri M., Cusano M., Gangarossa S., Caridi G., Bordo D., Lo Nigro C., Ghiggeri G.M., Ravazzolo R., Savino M., Del Vecchio M., d'Apolito M., Iolascon A., Zelante L.L., Savoia A., Balduini C.L., Noris P., Magrini U., Belletti S. , Heath K.E., Babcock M., Glucksman M.J., Aliprandis E., Bizzaro N., Desnick R.J., Martignetti J.A. Nat. Genet. 26:103-105(2000) [PubMed: 10973259] [Abstract] Cited for: VARIANTS MHA/FTNS/SBS LYS-93; CYS-702; CYS-1165; HIS-1424 AND LYS-1841.
[21]	"Mutation of MYH9, encoding non-muscle myosin heavy chain A, in May-Hegglin anomaly." Kelley M.J., Jawien W., Ortel T.L., Korczak J.F. Nat. Genet. 26:106-108(2000) [PubMed: 10973260] [Abstract] Cited for: VARIANTS MHA ILE-1155 AND LYS-1841.
[22]	"Nonmuscle myosin heavy chain IIA mutations define a spectrum of autosomal dominant macrothrombocytopenias: May-Hegglin anomaly and Fechtner, Sebastian, Epstein, and Alport-like syndromes." Heath K.E., Campos-Barros A., Toren A., Rozenfeld-Granot G., Carlsson L.E., Savige J., Denison J.C., Gregory M.C., White J.G., Barker D.F., Greinacher A., Epstein C.J., Glucksman M.J., Martignetti J.A. Am. J. Hum. Genet. 69:1033-1045(2001) [PubMed: 11590545] [Abstract] Cited for: VARIANTS MHA/SBS/FTNS/EPS/APSM ASN-373; CYS-702; HIS-702; PRO-1114; ASN-1424; HIS-1424 AND LYS-1841.
[23]	"Identification of six novel MYH9 mutations and genotype-phenotype relationships in autosomal dominant macrothrombocytopenia with leukocyte inclusions." Kunishima S., Matsushita T., Kojima T., Amemiya N., Choi Y.M., Hosaka N., Inoue M., Jung Y., Mamiya S., Matsumoto K., Miyajima Y., Zhang G., Ruan C., Saito K., Song K.S., Yoon H.-J., Kamiya T., Saito H. J. Hum. Genet. 46:722-729(2001) [PubMed: 11776386] [Abstract] Cited for: VARIANTS MHA/FTNS/SBS THR-95; CYS-1165; LEU-1165; 1205-LEU--GLN-1207 DEL; HIS-1424; ASN-1424; TYR-1424 AND LYS-1841, VARIANT VAL-1626.
[24]	"Epstein syndrome: another renal disorder with mutations in the nonmuscle myosin heavy chain 9 gene." Seri M., Savino M., Bordo D., Cusano R., Rocca B., Meloni I., Di Bari F., Koivisto P.A., Bolognesi M., Ghiggeri G.M., Landolfi R., Balduini C.L., Zelante L., Ravazzolo R., Renieri A., Savoia A. Hum. Genet. 110:182-186(2002) [PubMed: 11935325] [Abstract] Cited for: VARIANT EPS HIS-702.
[25]	"Expression of the nonmuscle myosin heavy chain IIA in the human kidney and screening for MYH9 mutations in Epstein and Fechtner syndromes." Arrondel C., Vodovar N., Knebelmann B., Gruenfeld J.-P., Gubler M.-C., Antignac C., Heidet L. J. Am. Soc. Nephrol. 13:65-74(2002) [PubMed: 11752022] [Abstract] Cited for: VARIANTS FTNS/EPS LEU-96; LEU-1165; ASN-1424 AND LYS-1841, VARIANT TRP-1400, TISSUE SPECIFICITY.
[26]	"Asp1424Asn MYH9 mutation results in an unstable protein responsible for the phenotypes in May-Hegglin anomaly/Fechtner syndrome." Deutsch S., Rideau A., Bochaton-Piallat M.-L., Merla G., Geinoz A., Gabbiani G., Schwede T., Matthes T., Antonarakis S.E., Beris P. Blood 102:529-534(2003) [PubMed: 12649151] [Abstract] Cited for: CHARACTERIZATION OF VARIANT ASN-1424.
[27]	"Immunofluorescence analysis of neutrophil nonmuscle myosin heavy chain-A in MYH9 disorders: association of subcellular localization with MYH9 mutations." Kunishima S., Matsushita T., Kojima T., Sako M., Kimura F., Jo E.-K., Inoue C., Kamiya T., Saito H. Lab. Invest. 83:115-122(2003) [PubMed: 12533692] [Abstract] Cited for: VARIANT FTNS/SBS CYS-1165, VARIANTS SBS LEU-1165 AND 1205-LEU--GLN-1207 DEL, VARIANTS MHA HIS-1424; ASN-1424; TYR-1424 AND LYS-1841, VARIANT EPS VAL-1816, VARIANT FTNS/MHA LYS-1841.
[28]	"MYH9-related disease: may-Hegglin anomaly, Sebastian syndrome, Fechtner syndrome, and Epstein syndrome are not distinct entities but represent a variable expression of a single illness." Seri M., Pecci A., Di Bari F., Cusano R., Savino M., Panza E., Nigro A., Noris P., Gangarossa S., Rocca B., Gresele P., Bizzaro N., Malatesta P., Koivisto P.A., Longo I., Musso R., Pecoraro C., Iolascon A. , Magrini U., Rodriguez Soriano J., Renieri A., Ghiggeri G.M., Ravazzolo R., Balduini C.L., Savoia A. Medicine (Baltimore) 82:203-215(2003) [PubMed: 12792306] [Abstract] Cited for: VARIANT EPS HIS-702, VARIANTS FTNS GLN-910; ILE-1155 AND HIS-1424, VARIANTS MHA/SBS 1066-GLU--ALA-1072 DEL AND ASN-1424, VARIANT EPS/FTNS/MHA/SBS CYS-702.
[29]	"Macrothrombocytopenia and progressive deafness is due to a mutation in MYH9." Mhatre A.N., Kim Y., Brodie H.A., Lalwani A.K. Otol. Neurotol. 24:205-209(2003) [PubMed: 12621333] [Abstract] Cited for: VARIANT MPSD ASN-1424.
[30]	"Bladder exstrophy and Epstein type congenital macrothrombocytopenia: evidence for a common cause?" Utsch B., DiFeo A., Kujat A., Karle S., Schuster V., Lenk H., Jacobs U., Mueller M., Doetsch J., Rascher W., Reutter H., Martignetti J.A., Ludwig M., Troebs R.-B. Am. J. Med. Genet. A 140:2251-2253(2006) [PubMed: 16969870] [Abstract] Cited for: VARIANT EPS LEU-96.
[31]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-810.
[32]	"Position of nonmuscle myosin heavy chain IIA (NMMHC-IIA) mutations predicts the natural history of MYH9-related disease." Pecci A., Panza E., Pujol-Moix N., Klersy C., Di Bari F., Bozzi V., Gresele P., Lethagen S., Fabris F., Dufour C., Granata A., Doubek M., Pecoraro C., Koivisto P.A., Heller P.G., Iolascon A., Alvisi P., Schwabe D. , De Candia E., Rocca B., Russo U., Ramenghi U., Noris P., Seri M., Balduini C.L., Savoia A. Hum. Mutat. 29:409-417(2008) [PubMed: 18059020] [Abstract] Cited for: POSITION OF MUTATIONS IN MYH9-RELATED DISEASE.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR456526 mRNA. Translation: CAG30412.1. AL832639 mRNA. Translation: CAD89954.1. Frameshift. Z82215 Genomic DNA. Translation: CAB05105.1. M81105 mRNA. Translation: AAA59888.1. M69180 mRNA. Translation: AAA61765.1. M31013 mRNA. Translation: AAA36349.1.
IPI	IPI00019502. IPI00395772.
PIR	A61231.
RefSeq	NP_002464.1.
UniGene	Hs.474751
3D structure databases
HSSP	HSSP built from PDB template 1BR2 based on UniProtKB P10587.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35579. 22 interactions.
PTM databases
PhosphoSite	P35579.
Proteomic databases
PeptideAtlas	P35579.
PRIDE	P35579.
Genome annotation databases
Ensembl	ENSG00000100345. Homo sapiens. [Contig view]
GeneID	4627.
KEGG	hsa:4627.
Organism-specific databases
GeneCards	GC22M035001.
H-InvDB	HIX0016424.
HGNC	HGNC:7579. MYH9.
HPA	CAB015386. HPA001644.
MIM	153640. phenotype. 153650. phenotype. 155100. phenotype. 160775. gene. 600208. phenotype. 603622. phenotype. 605249. phenotype.
Orphanet	90635. Deafness, autosomal dominant, nonsyndromic, sensorineural, type DFNA. 1019. Epstein syndrome. 1984. Fechtner syndrome. 850. May-Hegglin thrombocytopenia. 87884. Nonsyndromic genetic deafness. 807. Sebastian syndrome.
PharmGKB	PA31377.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P35579.
HOVERGEN	P35579.
OMA	P35579. KHSQAVE.
Gene expression databases
ArrayExpress	P35579.
Bgee	P35579.
CleanEx	HS_MYH9.
GermOnline	ENSG00000100345. Homo sapiens.
Family and domain databases
InterPro	IPR000048. IQ_CaM_bd_region. IPR001609. Myosin_head. IPR004009. Myosin_N. IPR002928. Myosin_tail. [Graphical view]
Pfam	PF00612. IQ. 1 hit. PF00063. Myosin_head. 1 hit. PF02736. Myosin_N. 1 hit. PF01576. Myosin_tail_1. 1 hit. [Graphical view]
PRINTS	PR00193. MYOSINHEAVY.
ProDom	PD000355. Myosin_head. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00015. IQ. 1 hit. SM00242. MYSc. 1 hit. [Graphical view]
PROSITE	PS50096. IQ. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	17810.
PMAP-CutDB	P35579.
SOURCE	Search...

Entry information

Entry name

MYH9_HUMAN

Accession

Primary (citable) accession number: P35579
Secondary accession number(s): O60805, Q86T83

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 113 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)