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P35579

- MYH9_HUMAN

UniProt

P35579 - MYH9_HUMAN

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Protein

Myosin-9

Gene

MYH9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi174 – 1818ATPSequence Analysis

GO - Molecular functioni

  1. actin binding Source: MGI
  2. actin-dependent ATPase activity Source: MGI
  3. actin filament binding Source: UniProtKB
  4. ADP binding Source: MGI
  5. ATPase activity Source: UniProtKB
  6. ATP binding Source: MGI
  7. microfilament motor activity Source: UniProtKB
  8. motor activity Source: UniProtKB
  9. poly(A) RNA binding Source: UniProtKB
  10. protein anchor Source: UniProtKB
  11. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. actin filament-based movement Source: UniProtKB
  3. actomyosin structure organization Source: UniProt
  4. angiogenesis Source: UniProtKB
  5. ATP catabolic process Source: UniProt
  6. axon guidance Source: Reactome
  7. blood vessel endothelial cell migration Source: UniProtKB
  8. cytokinesis Source: UniProtKB
  9. establishment of meiotic spindle localization Source: Ensembl
  10. establishment of T cell polarity Source: Ensembl
  11. integrin-mediated signaling pathway Source: UniProtKB
  12. in utero embryonic development Source: Ensembl
  13. leukocyte migration Source: UniProtKB
  14. meiotic spindle organization Source: Ensembl
  15. membrane protein ectodomain proteolysis Source: UniProtKB
  16. monocyte differentiation Source: UniProtKB
  17. myoblast fusion Source: Ensembl
  18. platelet aggregation Source: UniProtKB
  19. platelet formation Source: UniProtKB
  20. protein transport Source: UniProtKB
  21. regulation of cell shape Source: UniProtKB
  22. termination of G-protein coupled receptor signaling pathway Source: InterPro
  23. uropod organization Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

Cell adhesion, Cell shape

Keywords - Ligandi

Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.

Names & Taxonomyi

Protein namesi
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 namesi
Name:MYH9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:7579. MYH9.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity
Note: Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells.1 Publication

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. actomyosin Source: UniProt
  3. actomyosin contractile ring Source: UniProtKB
  4. cell-cell adherens junction Source: Ensembl
  5. cell leading edge Source: UniProtKB
  6. cleavage furrow Source: UniProtKB
  7. cortical cytoskeleton Source: Ensembl
  8. cytoplasm Source: UniProtKB
  9. cytosol Source: UniProtKB
  10. extracellular vesicular exosome Source: UniProtKB
  11. immunological synapse Source: Ensembl
  12. membrane Source: UniProtKB
  13. myosin II complex Source: UniProt
  14. myosin II filament Source: UniProt
  15. neuromuscular junction Source: Ensembl
  16. nucleus Source: UniProtKB
  17. plasma membrane Source: UniProtKB
  18. protein complex Source: UniProtKB
  19. ruffle Source: UniProtKB
  20. spindle Source: Ensembl
  21. stress fiber Source: UniProtKB
  22. uropod Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931N → K in MHA. 1 Publication
VAR_010791
Natural varianti95 – 951A → T in MHA. 1 Publication
VAR_018308
Natural varianti373 – 3731K → N in MHA and SBS. 1 Publication
VAR_018310
Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
VAR_010792
Natural varianti1066 – 10727Missing in MHA and SBS. 1 Publication
VAR_044228
Natural varianti1155 – 11551T → I in MHA and FTNS. 2 Publications
VAR_010794
Natural varianti1165 – 11651R → L in FTNS, MHA and SBS. 3 Publications
VAR_018313
Natural varianti1424 – 14241D → H in FTNS and MHA. 5 Publications
VAR_010796
Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 6 Publications
VAR_018316
Natural varianti1424 – 14241D → Y in MHA. 2 Publications
VAR_018317
Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
VAR_010797
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti373 – 3731K → N in MHA and SBS. 1 Publication
VAR_018310
Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
VAR_010792
Natural varianti1066 – 10727Missing in MHA and SBS. 1 Publication
VAR_044228
Natural varianti1165 – 11651R → C in FTNS and SBS. 3 Publications
VAR_010795
Natural varianti1165 – 11651R → L in FTNS, MHA and SBS. 3 Publications
VAR_018313
Natural varianti1205 – 12073Missing in SBS. 2 Publications
VAR_018314
Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 6 Publications
VAR_018316
Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
VAR_010797
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.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
VAR_010792
Natural varianti910 – 9101K → Q in FTNS. 1 Publication
VAR_044226
Natural varianti1155 – 11551T → I in MHA and FTNS. 2 Publications
VAR_010794
Natural varianti1165 – 11651R → C in FTNS and SBS. 3 Publications
VAR_010795
Natural varianti1165 – 11651R → L in FTNS, MHA and SBS. 3 Publications
VAR_018313
Natural varianti1424 – 14241D → H in FTNS and MHA. 5 Publications
VAR_010796
Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 6 Publications
VAR_018316
Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
VAR_010797
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
VAR_010792
Natural varianti702 – 7021R → H in APSM and EPS. 3 Publications
VAR_018311
Natural varianti1114 – 11141S → P in APSM. 1 Publication
VAR_018312
Epstein syndrome (EPS) [MIM:153650]: An autosomal dominant disorder characterized by the association of macrothrombocytopathy, sensorineural hearing loss and nephritis.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961S → L in EPS. 2 Publications
VAR_018309
Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
VAR_010792
Natural varianti702 – 7021R → H in APSM and EPS. 3 Publications
VAR_018311
Natural varianti1400 – 14001R → W in a EPS patient; might contribute to pathogenicity; when associated with L-96. 1 Publication
Corresponds to variant rs76368635 [ dbSNP | Ensembl ].
VAR_018315
Natural varianti1816 – 18161I → V in EPS. 1 Publication
VAR_030385
Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
VAR_010797
Deafness, autosomal dominant, 17 (DFNA17) [MIM:603622]: A form of deafness characterized by progressive high frequency hearing impairment and cochleosaccular degeneration.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti705 – 7051R → H in DFNA17. 1 Publication
VAR_010793
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 6 Publications
VAR_018316
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.
Genetic variations in MYH9 are associated with non-diabetic end stage renal disease (ESRD).

Keywords - Diseasei

Alport syndrome, Cataract, Deafness, Disease mutation, Non-syndromic deafness

Organism-specific databases

MIMi153640. phenotype.
153650. phenotype.
155100. phenotype.
600208. phenotype.
603622. phenotype.
605249. phenotype.
Orphaneti90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
182050. MYH9-related disease.
PharmGKBiPA31377.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 19601959Myosin-9PRO_0000123416Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei8 – 81N6-acetyllysine1 Publication
Modified residuei11 – 111Phosphotyrosine1 Publication
Modified residuei102 – 1021N6-acetyllysine1 Publication
Modified residuei299 – 2991N6-acetyllysine1 Publication
Modified residuei613 – 6131N6-acetyllysineBy similarity
Modified residuei754 – 7541PhosphotyrosineBy similarity
Modified residuei850 – 8501N6-succinyllysineBy similarity
Modified residuei860 – 8601N6-acetyllysineBy similarity
Modified residuei975 – 9751N6-acetyllysineBy similarity
Modified residuei1024 – 10241N6-acetyllysine1 Publication
Modified residuei1249 – 12491N6-acetyllysineBy similarity
Modified residuei1357 – 13571N6-acetyllysine1 Publication
Modified residuei1392 – 13921N6-acetyllysine1 Publication
Modified residuei1404 – 14041N6-acetyllysine1 Publication
Modified residuei1410 – 14101N6-acetyllysine1 Publication
Modified residuei1459 – 14591N6-acetyllysine1 Publication
Modified residuei1638 – 16381N6-acetyllysine1 Publication
Modified residuei1669 – 16691N6-succinyllysineBy similarity
Modified residuei1714 – 17141Phosphoserine1 Publication
Modified residuei1793 – 17931N6-acetyllysineBy similarity
Modified residuei1802 – 18021N6-acetyllysineBy similarity
Modified residuei1845 – 18451N6-acetyllysineBy similarity
Modified residuei1943 – 19431Phosphoserine10 Publications

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP35579.
PaxDbiP35579.
PeptideAtlasiP35579.
PRIDEiP35579.

PTM databases

PhosphoSiteiP35579.

Miscellaneous databases

PMAP-CutDBP35579.

Expressioni

Tissue specificityi

In the kidney, expressed in the glomeruli. Also expressed in leukocytes.2 Publications

Gene expression databases

BgeeiP35579.
CleanExiHS_MYH9.
ExpressionAtlasiP35579. baseline and differential.
GenevestigatoriP35579.

Organism-specific databases

HPAiCAB015386.
HPA001644.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CXCR4P610735EBI-350338,EBI-489411
GRB2P629933EBI-350338,EBI-401755
MEN1O002557EBI-350338,EBI-592789
NCLP193383EBI-350338,EBI-346967
SVILO463852EBI-350338,EBI-6995105From a different organism.

Protein-protein interaction databases

BioGridi110712. 96 interactions.
DIPiDIP-33103N.
IntActiP35579. 49 interactions.
MINTiMINT-7901706.
STRINGi9606.ENSP00000216181.

Structurei

Secondary structure

1
1960
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1895 – 18973
Helixi1899 – 19035
Helixi1904 – 192118
Beta strandi1922 – 19254

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LNKNMR-C1897-1935[»]
3ZWHX-ray1.94Q1893-1937[»]
4CFQX-ray1.37Q/R1893-1937[»]
4CFRX-ray1.40Q1893-1937[»]
4ETOX-ray1.54P1908-1923[»]
ProteinModelPortaliP35579.
SMRiP35579. Positions 7-897, 1902-1930.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 776696Myosin motorAdd
BLAST
Domaini779 – 80830IQPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni654 – 67623Actin-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili837 – 19261090Sequence AnalysisAdd
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 IQ domain.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5022.
GeneTreeiENSGT00760000118919.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiP35579.
KOiK10352.
OMAiKRENDSI.
OrthoDBiEOG71CFK3.
PhylomeDBiP35579.
TreeFamiTF333601.

Family and domain databases

Gene3Di4.10.270.10. 1 hit.
InterProiIPR000048. 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.
[Graphical view]
PfamiPF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35579-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSDKSG FEPASLKEEV
60 70 80 90 100
GEEAIVELVE NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN
110 120 130 140 150
LKERYYSGLI YTYSGLFCVV INPYKNLPIY SEEIVEMYKG KKRHEMPPHI
160 170 180 190 200
YAITDTAYRS MMQDREDQSI LCTGESGAGK TENTKKVIQY LAYVASSHKS
210 220 230 240 250
KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR INFDVNGYIV
260 270 280 290 300
GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY
310 320 330 340 350
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEEEQMGLL RVISGVLQLG
360 370 380 390 400
NIVFKKERNT DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY
410 420 430 440 450
VQKAQTKEQA DFAIEALAKA TYERMFRWLV LRINKALDKT KRQGASFIGI
460 470 480 490 500
LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF NHTMFILEQE EYQREGIEWN
510 520 530 540 550
FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK SFVEKVMQEQ
560 570 580 590 600
GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL
610 620 630 640 650
HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY
660 670 680 690 700
KEQLAKLMAT LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG
710 720 730 740 750
IRICRQGFPN RVVFQEFRQR YEILTPNSIP KGFMDGKQAC VLMIKALELD
760 770 780 790 800
SNLYRIGQSK VFFRAGVLAH LEEERDLKIT DVIIGFQACC RGYLARKAFA
810 820 830 840 850
KRQQQLTAMK VLQRNCAAYL KLRNWQWWRL FTKVKPLLQV SRQEEEMMAK
860 870 880 890 900
EEELVKVREK QLAAENRLTE METLQSQLMA EKLQLQEQLQ AETELCAEAE
910 920 930 940 950
ELRARLTAKK QELEEICHDL EARVEEEEER CQHLQAEKKK MQQNIQELEE
960 970 980 990 1000
QLEEEESARQ KLQLEKVTTE AKLKKLEEEQ IILEDQNCKL AKEKKLLEDR
1010 1020 1030 1040 1050
IAEFTTNLTE EEEKSKSLAK LKNKHEAMIT DLEERLRREE KQRQELEKTR
1060 1070 1080 1090 1100
RKLEGDSTDL SDQIAELQAQ IAELKMQLAK KEEELQAALA RVEEEAAQKN
1110 1120 1130 1140 1150
MALKKIRELE SQISELQEDL ESERASRNKA EKQKRDLGEE LEALKTELED
1160 1170 1180 1190 1200
TLDSTAAQQE LRSKREQEVN ILKKTLEEEA KTHEAQIQEM RQKHSQAVEE
1210 1220 1230 1240 1250
LAEQLEQTKR VKANLEKAKQ TLENERGELA NEVKVLLQGK GDSEHKRKKV
1260 1270 1280 1290 1300
EAQLQELQVK FNEGERVRTE LADKVTKLQV ELDNVTGLLS QSDSKSSKLT
1310 1320 1330 1340 1350
KDFSALESQL QDTQELLQEE NRQKLSLSTK LKQVEDEKNS FREQLEEEEE
1360 1370 1380 1390 1400
AKHNLEKQIA TLHAQVADMK KKMEDSVGCL ETAEEVKRKL QKDLEGLSQR
1410 1420 1430 1440 1450
HEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSACNLE KKQKKFDQLL
1460 1470 1480 1490 1500
AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK
1510 1520 1530 1540 1550
QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA
1560 1570 1580 1590 1600
TEDAKLRLEV NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED
1610 1620 1630 1640 1650
ERKQRSMAVA ARKKLEMDLK DLEAHIDSAN KNRDEAIKQL RKLQAQMKDC
1660 1670 1680 1690 1700
MRELDDTRAS REEILAQAKE NEKKLKSMEA EMIQLQEELA AAERAKRQAQ
1710 1720 1730 1740 1750
QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE EQGNTELIND
1760 1770 1780 1790 1800
RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KVKLQEMEGT
1810 1820 1830 1840 1850
VKSKYKASIT ALEAKIAQLE EQLDNETKER QAACKQVRRT EKKLKDVLLQ
1860 1870 1880 1890 1900
VDDERRNAEQ YKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL
1910 1920 1930 1940 1950
EDATETADAM NREVSSLKNK LRRGDLPFVV PRRMARKGAG DGSDEEVDGK
1960
ADGAEAKPAE
Length:1,960
Mass (Da):226,532
Last modified:January 23, 2007 - v4
Checksum:i588F84BB8C106E6F
GO
Isoform 2 (identifier: P35579-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,382
Mass (Da):159,864
Checksum:i02727B4F964F5839
GO

Sequence cautioni

The sequence CAD89954.1 differs from that shown. Reason: Frameshift at position 1890.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 553EAI → RGH(PubMed:1860190)Curated
Sequence conflicti660 – 6601T → S(PubMed:1860190)Curated
Sequence conflicti869 – 8691T → M in AAA36349. (PubMed:1967836)Curated
Sequence conflicti931 – 9311C → Y in AAA36349. (PubMed:1967836)Curated
Sequence conflicti1000 – 10001R → I in BAF84298. (PubMed:14702039)Curated
Sequence conflicti1240 – 12412KG → GR in AAA36349. (PubMed:1967836)Curated
Sequence conflicti1350 – 13501E → EE(PubMed:1967836)Curated
Sequence conflicti1462 – 14621E → G in CAD89954. (PubMed:15461802)Curated
Sequence conflicti1546 – 15461D → G in CAD89954. (PubMed:15461802)Curated
Sequence conflicti1764 – 17641T → A in AAA36349. (PubMed:1967836)Curated
Sequence conflicti1771 – 17711S → G in AAA36349. (PubMed:1967836)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931N → K in MHA. 1 Publication
VAR_010791
Natural varianti95 – 951A → T in MHA. 1 Publication
VAR_018308
Natural varianti96 – 961S → L in EPS. 2 Publications
VAR_018309
Natural varianti373 – 3731K → N in MHA and SBS. 1 Publication
VAR_018310
Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
VAR_010792
Natural varianti702 – 7021R → H in APSM and EPS. 3 Publications
VAR_018311
Natural varianti705 – 7051R → H in DFNA17. 1 Publication
VAR_010793
Natural varianti810 – 8101K → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_036006
Natural varianti910 – 9101K → Q in FTNS. 1 Publication
VAR_044226
Natural varianti967 – 9671V → E.
Corresponds to variant rs16996652 [ dbSNP | Ensembl ].
VAR_044227
Natural varianti1066 – 10727Missing in MHA and SBS. 1 Publication
VAR_044228
Natural varianti1114 – 11141S → P in APSM. 1 Publication
VAR_018312
Natural varianti1155 – 11551T → I in MHA and FTNS. 2 Publications
VAR_010794
Natural varianti1165 – 11651R → C in FTNS and SBS. 3 Publications
VAR_010795
Natural varianti1165 – 11651R → L in FTNS, MHA and SBS. 3 Publications
VAR_018313
Natural varianti1205 – 12073Missing in SBS. 2 Publications
VAR_018314
Natural varianti1400 – 14001R → W in a EPS patient; might contribute to pathogenicity; when associated with L-96. 1 Publication
Corresponds to variant rs76368635 [ dbSNP | Ensembl ].
VAR_018315
Natural varianti1424 – 14241D → H in FTNS and MHA. 5 Publications
VAR_010796
Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 6 Publications
VAR_018316
Natural varianti1424 – 14241D → Y in MHA. 2 Publications
VAR_018317
Natural varianti1626 – 16261I → V.1 Publication
Corresponds to variant rs2269529 [ dbSNP | Ensembl ].
VAR_018318
Natural varianti1816 – 18161I → V in EPS. 1 Publication
VAR_030385
Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
VAR_010797

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 136136Missing in isoform 2. 1 PublicationVSP_035409Add
BLAST
Alternative sequencei980 – 1421442Missing in isoform 2. 1 PublicationVSP_035410Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR456526 mRNA. Translation: CAG30412.1.
AB191263 mRNA. Translation: BAD52439.1.
AL832639 mRNA. Translation: CAD89954.1. Frameshift.
AB290175 mRNA. Translation: BAG06729.1.
Z82215 Genomic DNA. Translation: CAB05105.1.
CH471095 Genomic DNA. Translation: EAW60096.1.
M81105 mRNA. Translation: AAA59888.1.
AK291609 mRNA. Translation: BAF84298.1.
M69180 mRNA. Translation: AAA61765.1.
M31013 mRNA. Translation: AAA36349.1.
CCDSiCCDS13927.1. [P35579-1]
PIRiA61231.
RefSeqiNP_002464.1. NM_002473.5. [P35579-1]
UniGeneiHs.474751.

Genome annotation databases

EnsembliENST00000216181; ENSP00000216181; ENSG00000100345. [P35579-1]
GeneIDi4627.
KEGGihsa:4627.
UCSCiuc003apg.3. human. [P35579-1]

Polymorphism databases

DMDMi6166599.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR456526 mRNA. Translation: CAG30412.1 .
AB191263 mRNA. Translation: BAD52439.1 .
AL832639 mRNA. Translation: CAD89954.1 . Frameshift.
AB290175 mRNA. Translation: BAG06729.1 .
Z82215 Genomic DNA. Translation: CAB05105.1 .
CH471095 Genomic DNA. Translation: EAW60096.1 .
M81105 mRNA. Translation: AAA59888.1 .
AK291609 mRNA. Translation: BAF84298.1 .
M69180 mRNA. Translation: AAA61765.1 .
M31013 mRNA. Translation: AAA36349.1 .
CCDSi CCDS13927.1. [P35579-1 ]
PIRi A61231.
RefSeqi NP_002464.1. NM_002473.5. [P35579-1 ]
UniGenei Hs.474751.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LNK NMR - C 1897-1935 [» ]
3ZWH X-ray 1.94 Q 1893-1937 [» ]
4CFQ X-ray 1.37 Q/R 1893-1937 [» ]
4CFR X-ray 1.40 Q 1893-1937 [» ]
4ETO X-ray 1.54 P 1908-1923 [» ]
ProteinModelPortali P35579.
SMRi P35579. Positions 7-897, 1902-1930.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110712. 96 interactions.
DIPi DIP-33103N.
IntActi P35579. 49 interactions.
MINTi MINT-7901706.
STRINGi 9606.ENSP00000216181.

Chemistry

ChEMBLi CHEMBL2189151.

PTM databases

PhosphoSitei P35579.

Polymorphism databases

DMDMi 6166599.

Proteomic databases

MaxQBi P35579.
PaxDbi P35579.
PeptideAtlasi P35579.
PRIDEi P35579.

Protocols and materials databases

DNASUi 4627.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216181 ; ENSP00000216181 ; ENSG00000100345 . [P35579-1 ]
GeneIDi 4627.
KEGGi hsa:4627.
UCSCi uc003apg.3. human. [P35579-1 ]

Organism-specific databases

CTDi 4627.
GeneCardsi GC22M036677.
GeneReviewsi MYH9.
HGNCi HGNC:7579. MYH9.
HPAi CAB015386.
HPA001644.
MIMi 153640. phenotype.
153650. phenotype.
155100. phenotype.
160775. gene.
600208. phenotype.
603622. phenotype.
605249. phenotype.
neXtProti NX_P35579.
Orphaneti 90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
182050. MYH9-related disease.
PharmGKBi PA31377.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5022.
GeneTreei ENSGT00760000118919.
HOGENOMi HOG000173958.
HOVERGENi HBG004704.
InParanoidi P35579.
KOi K10352.
OMAi KRENDSI.
OrthoDBi EOG71CFK3.
PhylomeDBi P35579.
TreeFami TF333601.

Enzyme and pathway databases

Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.

Miscellaneous databases

ChiTaRSi MYH9. human.
GeneWikii MYH9.
GenomeRNAii 4627.
NextBioi 17810.
PMAP-CutDB P35579.
PROi P35579.
SOURCEi Search...

Gene expression databases

Bgeei P35579.
CleanExi HS_MYH9.
ExpressionAtlasi P35579. baseline and differential.
Genevestigatori P35579.

Family and domain databases

Gene3Di 4.10.270.10. 1 hit.
InterProi 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.
[Graphical view ]
Pfami PF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view ]
PRINTSi PR00193. MYOSINHEAVY.
SMARTi SM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view ]
SUPFAMi SSF48097. SSF48097. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  2. "Vector-capping: a simple method for preparing a high-quality full-length cDNA library."
    Kato S., Ohtoko K., Ohtake H., Kimura T.
    DNA Res. 12:53-62(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Spinal cord.
  4. "Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free recombination: Preparation of full-lemgth cDNA clones encoding motor proteins."
    Yamakawa H., Kikuno R.F., Nagase T., Ohara O.
    Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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.
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1009.
    Tissue: Placenta.
  9. "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.
  10. Bienvenut W.V., Claeys R.
    Submitted (AUG-2005) to UniProtKB
    Tissue: Platelet.
  11. "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.
  12. Cited for: INTERACTION WITH SVIL.
  13. Cited for: ISGYLATION.
  14. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  17. "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.
  18. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  20. Cited for: ASSOCIATION WITH END STAGE RENAL DISEASE.
  21. Cited for: ASSOCIATION WITH END STAGE RENAL DISEASE.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "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.
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  28. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading."
    Betapudi V.
    PLoS ONE 5:E8560-E8560(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  30. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "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.
  34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "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.
  36. Cited for: VARIANTS MHA/FTNS/SBS LYS-93; CYS-702; CYS-1165; HIS-1424 AND LYS-1841.
  37. "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.
  38. "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.
  39. "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.
  40. Cited for: VARIANT EPS HIS-702.
  41. "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.
  42. "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.
  43. "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.
  44. "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.
  45. "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.
  46. "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.
  47. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-810.
  48. Cited for: POSITION OF MUTATIONS IN MYH9-RELATED DISEASE.

Entry informationi

Entry nameiMYH9_HUMAN
AccessioniPrimary (citable) accession number: P35579
Secondary accession number(s): A8K6E4
, O60805, Q60FE2, Q86T83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 176 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3