P35579 (MYH9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myosin-9

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

Gene names

Name:

MYH9

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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. Interacts with SLC6A4 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). Interacts with RASIP1. Interacts with DDR1 By similarity. Interacts with SVIL and HTRA3. Ref.8 Ref.13 Ref.27
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cytoplasm › cell cortex By similarity. Note: Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells By similarity.
Tissue specificity	In the kidney, expressed in the glomeruli. Also expressed in leukocytes. Ref.4 Ref.34
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.
Post-translational modification	ISGylated. Ref.9
Involvement in disease	May-Hegglin anomaly (MHA) [MIM:155100]: A disorder characterized by thrombocytopenia, giant platelets and Dohle body-like inclusions in peripheral blood leukocytes. appearing as highly parallel paracrystalline bodies. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17 Ref.20 Ref.29 Ref.30 Ref.31 Ref.32 Ref.36 Ref.37 Ref.41 Sebastian syndrome (SBS) [MIM:605249]: Autosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukocyte inclusions that are smaller and less organized than in May-Hegglin anomaly. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17 Ref.20 Ref.36 Ref.41 Fechtner syndrome (FTNS) [MIM:153640]: 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17 Ref.20 Ref.34 Ref.36 Ref.37 Ref.41 Alport syndrome, with macrothrombocytopenia (APSM) [MIM:153650]: An autosomal dominant disorder characterized by the association of ocular lesions, sensorineural hearing loss and nephritis (Alport syndrome) with platelet defects. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17 Ref.20 Ref.41 Epstein syndrome (EPS) [MIM:153650]: An autosomal dominant disorder characterized by the association of macrothrombocytopathy, sensorineural hearing loss and nephritis. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17 Ref.20 Ref.33 Ref.36 Ref.37 Ref.39 Ref.41 Deafness, autosomal dominant, 17 (DFNA17) [MIM:603622]: A form of deafness characterized by progressive high frequency hearing impairment and cochleosaccular degeneration. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17 Ref.20 Ref.28 Ref.41 Macrothrombocytopenia and progressive sensorineural deafness (MPSD) [MIM:600208]: An autosomal dominant disorder characterized by the association of macrothrombocytopathy and progressive sensorineural hearing loss without renal dysfunction. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17 Ref.20 Ref.38 Ref.41 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.16 Ref.17 Ref.20 Ref.41 Genetic variations in MYH9 are associated with non-diabetic end stage renal disease (ESRD). Ref.16 Ref.17 Ref.20 Ref.41
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
Cellular component	Cytoplasm Cytoskeleton
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 Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton reorganization Inferred from mutant phenotype PubMed 15869600. Source: UniProtKB actin filament-based movement Inferred from direct assay PubMed 12237319. Source: UniProtKB angiogenesis Inferred from direct assay PubMed 16403913. Source: UniProtKB axon guidance Traceable author statement. Source: Reactome blood vessel endothelial cell migration Inferred from mutant phenotype PubMed 16403913. Source: UniProtKB cell-cell adhesion Inferred from electronic annotation. Source: Compara cytokinesis Inferred from mutant phenotype PubMed 15774463. Source: UniProtKB establishment of T cell polarity Inferred from electronic annotation. Source: Compara establishment of meiotic spindle localization Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara integrin-mediated signaling pathway Non-traceable author statement PubMed 10822899. Source: UniProtKB leukocyte migration Non-traceable author statement PubMed 12421915. Source: UniProtKB meiotic metaphase I Inferred from electronic annotation. Source: Compara meiotic spindle organization Inferred from electronic annotation. Source: Compara membrane protein ectodomain proteolysis Inferred from direct assay PubMed 16186248. Source: UniProtKB monocyte differentiation Inferred from expression pattern Ref.4. Source: UniProtKB myoblast fusion Inferred from electronic annotation. Source: Compara platelet formation Inferred from mutant phenotype PubMed 12237319. Source: UniProtKB protein transport Inferred from mutant phenotype PubMed 16403913. Source: UniProtKB regulation of cell shape Inferred from mutant phenotype PubMed 11029059. Source: UniProtKB termination of G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro uropod organization Inferred from electronic annotation. Source: Compara
Cellular_component	actomyosin contractile ring Inferred from direct assay PubMed 11029059. Source: UniProtKB cell-cell adherens junction Inferred from electronic annotation. Source: Compara cleavage furrow Inferred from direct assay PubMed 14508515PubMed 7699007. Source: UniProtKB cortical cytoskeleton Inferred from electronic annotation. Source: Compara cytosol Inferred from direct assay PubMed 14508515. Source: UniProtKB extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB immunological synapse Inferred from electronic annotation. Source: Compara myosin II complex Inferred from electronic annotation. Source: Compara neuromuscular junction Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 14508515. Source: UniProtKB plasma membrane Inferred from direct assay PubMed 16186248PubMed 16403913. Source: UniProtKB protein complex Inferred from direct assay PubMed 12421915. Source: UniProtKB ruffle Inferred from direct assay PubMed 16403913. Source: UniProtKB spindle Inferred from electronic annotation. Source: Compara stress fiber Inferred from direct assay PubMed 14508515PubMed 14706930PubMed 16403913PubMed 7699007. Source: UniProtKB uropod Inferred from direct assay PubMed 15064761. Source: MGI
Molecular_function	ADP binding Inferred from direct assay PubMed 15065866. Source: MGI ATP binding Inferred from direct assay PubMed 15065866PubMed 15845534. Source: MGI actin filament binding Inferred from direct assay PubMed 12237319PubMed 14508515. Source: UniProtKB actin-dependent ATPase activity Inferred from direct assay PubMed 15065866PubMed 15845534. Source: MGI microfilament motor activity Inferred from direct assay PubMed 12237319. Source: UniProtKB protein anchor Inferred from mutant phenotype PubMed 16403913. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 12237319. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CXCR4	P61073	5	EBI-350338,EBI-489411
MEN1	O00255	7	EBI-350338,EBI-592789
NCL	P19338	3	EBI-350338,EBI-346967

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 Ref.23

Modified residue

8

1

N6-acetyllysine Ref.23

Modified residue

11

1

Phosphotyrosine Ref.22

Modified residue

102

1

N6-acetyllysine Ref.23

Modified residue

181

1

Phosphothreonine By similarity

Modified residue

299

1

N6-acetyllysine Ref.23

Modified residue

638

1

Phosphothreonine By similarity

Modified residue

754

1

Phosphotyrosine By similarity

Modified residue

1024

1

N6-acetyllysine Ref.23

Modified residue

1357

1

N6-acetyllysine Ref.23

Modified residue

1392

1

N6-acetyllysine Ref.23

Modified residue

1404

1

N6-acetyllysine Ref.23

Modified residue

1410

1

N6-acetyllysine Ref.23

Modified residue

1459

1

N6-acetyllysine Ref.23

Modified residue

1638

1

N6-acetyllysine Ref.23

Modified residue

1714

1

Phosphoserine Ref.24

Modified residue

1943

1

Phosphoserine Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.19 Ref.21 Ref.22 Ref.24 Ref.26

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.29

VAR_010791

Natural variant

95

1

A → T in MHA. Ref.32

VAR_018308

Natural variant

96

1

S → L in EPS. Ref.34 Ref.39

VAR_018309

Natural variant

373

1

K → N in MHA and SBS. Ref.31

VAR_018310

Natural variant

702

1

R → C in APSM, EPS, FTNS, MHA and SBS. Ref.29 Ref.31 Ref.37

VAR_010792

Natural variant

702

1

R → H in APSM and EPS. Ref.31 Ref.33 Ref.37

VAR_018311

Natural variant

705

1

R → H in DFNA17. Ref.28

VAR_010793

Natural variant

810

1

K → N in a breast cancer sample; somatic mutation. Ref.40

VAR_036006

Natural variant

910

1

K → Q in FTNS. Ref.37

VAR_044226

Natural variant

967

1

V → E.
Corresponds to variant rs16996652 [ dbSNP | Ensembl ].

VAR_044227

Natural variant

1066 – 1072

7

Missing in MHA and SBS.

VAR_044228

Natural variant

1114

1

S → P in APSM. Ref.31

VAR_018312

Natural variant

1155

1

T → I in MHA and FTNS. Ref.30 Ref.37

VAR_010794

Natural variant

1165

1

R → C in FTNS and SBS. Ref.29 Ref.32 Ref.36

VAR_010795

Natural variant

1165

1

R → L in FTNS, MHA and SBS. Ref.32 Ref.34 Ref.36

VAR_018313

Natural variant

1205 – 1207

3

Missing in SBS.

VAR_018314

Natural variant

1400

1

R → W in a EPS patient; might contribute to pathogenicity; when associated with L-96. Ref.34

VAR_018315

Natural variant

1424

1

D → H in FTNS and MHA. Ref.29 Ref.31 Ref.32 Ref.36 Ref.37

VAR_010796

Natural variant

1424

1

D → N in FTNS, MHA, SBS and MPSD; affects protein stability. Ref.31 Ref.32 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38

VAR_018316

Natural variant

1424

1

D → Y in MHA. Ref.32 Ref.36

VAR_018317

Natural variant

1626

1

I → V. Ref.32
Corresponds to variant rs2269529 [ dbSNP | Ensembl ].

VAR_018318

Natural variant

1816

1

I → V in EPS. Ref.36

VAR_030385

Natural variant

1841

1

E → K in FTNS, SBS, MHA and EPS. Ref.29 Ref.30 Ref.31 Ref.32 Ref.34 Ref.36

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

1960

Helix Strand Turn

Details...

Beta strand

1895 – 1898

4

Helix

1899 – 1903

5

Turn

1904 – 1906

3

Helix

1909 – 1918

10

Beta strand

1922 – 1925

4

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 [UniParc]. 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:R84.1-R84.11(2004) [PubMed] [Europe PMC] [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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 714-1960.
[8]	"F-actin and myosin II binding domains in supervillin." Chen Y., Takizawa N., Crowley J.L., Oh S.W., Gatto C.L., Kambara T., Sato O., Li X.-D., Ikebe M., Luna E.J. J. Biol. Chem. 278:46094-46106(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SVIL.
[9]	"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ISGYLATION.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY. Tissue: Prostate cancer.
[13]	"Supervillin slows cell spreading by facilitating myosin II activation at the cell periphery." Takizawa N., Ikebe R., Ikebe M., Luna E.J. J. Cell Sci. 120:3792-3803(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SVIL.
[14]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY. Tissue: T-cell.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY. Tissue: Platelet.
[16]	"MYH9 is a major-effect risk gene for focal segmental glomerulosclerosis." Kopp J.B., Smith M.W., Nelson G.W., Johnson R.C., Freedman B.I., Bowden D.W., Oleksyk T., McKenzie L.M., Kajiyama H., Ahuja T.S., Berns J.S., Briggs W., Cho M.E., Dart R.A., Kimmel P.L., Korbet S.M., Michel D.M., Mokrzycki M.H. , Schelling J.R., Simon E., Trachtman H., Vlahov D., Winkler C.A. Nat. Genet. 40:1175-1184(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH END STAGE RENAL DISEASE.
[17]	"MYH9 is associated with nondiabetic end-stage renal disease in African Americans." Kao W.H., Klag M.J., Meoni L.A., Reich D., Berthier-Schaad Y., Li M., Coresh J., Patterson N., Tandon A., Powe N.R., Fink N.E., Sadler J.H., Weir M.R., Abboud H.E., Adler S.G., Divers J., Iyengar S.K., Freedman B.I. , Kimmel P.L., Knowler W.C., Kohn O.F., Kramp K., Leehey D.J., Nicholas S.B., Pahl M.V., Schelling J.R., Sedor J.R., Thornley-Brown D., Winkler C.A., Smith M.W., Parekh R.S. Nat. Genet. 40:1185-1192(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH END STAGE RENAL DISEASE.
[18]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[19]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY. Tissue: Liver.
[20]	"Polymorphisms in the non-muscle myosin heavy chain 9 gene (MYH9) are strongly associated with end-stage renal disease historically attributed to hypertension in African Americans." Freedman B.I., Hicks P.J., Bostrom M.A., Cunningham M.E., Liu Y., Divers J., Kopp J.B., Winkler C.A., Nelson G.W., Langefeld C.D., Bowden D.W. Kidney Int. 75:736-745(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH END STAGE RENAL DISEASE.
[21]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY.
[22]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11 AND SER-1943, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[23]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-8; LYS-102; LYS-299; LYS-1024; LYS-1357; LYS-1392; LYS-1404; LYS-1410; LYS-1459 AND LYS-1638, MASS SPECTROMETRY.
[24]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1714 AND SER-1943, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY.
[27]	"Application of the wheat-germ cell-free translation system to produce high temperature requirement A3 (HtrA3) proteases." Singh H., Makino S., Endo Y., Li Y., Stephens A.N., Nie G. BioTechniques 52:23-28(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HTRA3.
[28]	"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] [Europe PMC] [Abstract] Cited for: VARIANT DFNA17 HIS-705.
[29]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS MHA/FTNS/SBS LYS-93; CYS-702; CYS-1165; HIS-1424 AND LYS-1841.
[30]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS MHA ILE-1155 AND LYS-1841.
[31]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS MHA/SBS/FTNS/EPS/APSM ASN-373; CYS-702; HIS-702; PRO-1114; ASN-1424; HIS-1424 AND LYS-1841.
[32]	"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] [Europe PMC] [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.
[33]	"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] [Europe PMC] [Abstract] Cited for: VARIANT EPS HIS-702.
[34]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS FTNS/EPS LEU-96; LEU-1165; ASN-1424 AND LYS-1841, VARIANT TRP-1400, TISSUE SPECIFICITY.
[35]	"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] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT ASN-1424.
[36]	"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] [Europe PMC] [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.
[37]	"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] [Europe PMC] [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.
[38]	"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] [Europe PMC] [Abstract] Cited for: VARIANT MPSD ASN-1424.
[39]	"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] [Europe PMC] [Abstract] Cited for: VARIANT EPS LEU-96.
[40]	"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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-810.
[41]	"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] [Europe PMC] [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

EMBL
GenBank
DDBJ

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. NM_002473.4.

UniGene

Hs.474751.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LNK	NMR	-	C	1897-1935	[»]
3ZWH	X-ray	1.94	Q	1894-1937	[»]
4ETO	X-ray	1.54	P	1908-1923	[»]

ProteinModelPortal

P35579.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33103N.

IntAct

P35579. 38 interactions.

MINT

MINT-1147379.

STRING

9606.ENSP00000216181.

PTM databases

PhosphoSite

P35579.

Polymorphism databases

DMDM

6166599.

Proteomic databases

PaxDb

P35579.

PeptideAtlas

P35579.

PRIDE

P35579.

Protocols and materials databases

DNASU

4627.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216181; ENSP00000216181; ENSG00000100345.

GeneID

4627.

KEGG

hsa:4627.

UCSC

uc003apg.3. human.

Organism-specific databases

CTD

4627.

GeneCards

GC22M036677.

HGNC

HGNC:7579. MYH9.

HPA

CAB015386.
HPA001644.

MIM

153640. phenotype.
153650. phenotype.
155100. phenotype.
160775. gene.
600208. phenotype.
603622. phenotype.
605249. phenotype.

neXtProt

NX_P35579.

Orphanet

90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
1019. Epstein syndrome.
1984. Fechtner syndrome.
850. May-Hegglin thrombocytopenia.
807. Sebastian syndrome.

PharmGKB

PA31377.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5022.

HOGENOM

HOG000173958.

HOVERGEN

HBG004704.

InParanoid

P35579.

KO

K10352.

OMA

EMRQKHS.

OrthoDB

EOG4TXBR1.

PhylomeDB

P35579.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

P35579.

Bgee

P35579.

CleanEx

HS_MYH9.

Genevestigator

P35579.

GermOnline

ENSG00000100345. Homo sapiens.

Family and domain databases

InterPro

IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR002928. Myosin_tail.
IPR016137. Regulat_G_prot_signal_superfam.
[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.

SMART

SM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]

SUPFAM

SSF48097. Regulat_G_prot_signal_superfam. 1 hit.

PROSITE

PS50096. IQ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MYH9. human.

GenomeRNAi

4627.

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:	May 1, 2013
This is version 159 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.