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P35749 (MYH11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin-11
Alternative name(s):
Myosin heavy chain 11
Myosin heavy chain, smooth muscle isoform
SMMHC
Gene names
Name:MYH11
Synonyms:KIAA0866
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1972 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Muscle contraction.

Subunit structure

Muscle 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).

Subcellular location

Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Thick filaments of the myofibrils. Ref.11

Tissue specificity

Smooth muscle; expressed in the umbilical artery, bladder, esophagus and trachea. Isoform 1 is mostly found in slowly contracting tonic muscles. Ref.1

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.

Each myosin heavy chain can be split into 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). It can later be split further into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2).

Involvement in disease

A chromosomal aberration involving MYH11 is found in acute myeloid leukemia of M4EO subtype. Pericentric inversion inv16(p13;q22). The inversion produces a fusion protein consisting of the 165 N-terminal residues of CBF-beta (PEPB2) and the tail region of MYH11.

Aortic aneurysm, familial thoracic 4 (AAT4) [MIM:132900]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Sequence similarities

Contains 1 IQ domain.

Contains 1 myosin head-like domain.

Sequence caution

The sequence BAA74889.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentThick filament
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseAortic aneurysm
Disease mutation
Proto-oncogene
   DomainCoiled coil
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Muscle protein
Myosin
   PTMMethylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

cardiac muscle fiber development

Inferred from mutant phenotype Ref.14. Source: UniProtKB

elastic fiber assembly

Inferred from mutant phenotype Ref.14. Source: UniProtKB

muscle contraction

Traceable author statement. Source: Reactome

skeletal muscle myosin thick filament assembly

Inferred from sequence or structural similarity. Source: UniProtKB

smooth muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

muscle myosin complex

Traceable author statement Ref.9. Source: ProtInc

myosin filament

Inferred from electronic annotation. Source: UniProtKB-KW

smooth muscle contractile fiber

Inferred from electronic annotation. Source: Ensembl

stress fiber

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

motor activity

Inferred from electronic annotation. Source: Ensembl

structural constituent of muscle

Inferred from mutant phenotype Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MYL12BO149502EBI-1052928,EBI-1642165

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35749-1)

Also known as: SM-A;

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: P35749-2)

Also known as: SM-B1;

The sequence of this isoform differs from the canonical sequence as follows:
     211-211: T → TQGPSFAY
Note: This isoform with a 7 AA insert in the head domain is predominantly expressed in rapidly contracting phasic muscles.
Isoform 3 (identifier: P35749-3)

Also known as: SM-B2;

The sequence of this isoform differs from the canonical sequence as follows:
     211-211: T → TQGPSFAY
     1930-1972: RGNETSFVPSRRSGGRRVIENADGSEEETDTRDADFNGTKASE → GPPPQETSQ
Note: This isoform with a 7 AA insert in the head domain is predominantly expressed in rapidly contracting phasic muscles.
Isoform 4 (identifier: P35749-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1930-1972: RGNETSFVPSRRSGGRRVIENADGSEEETDTRDADFNGTKASE → GPPPQETSQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19721972Myosin-11
PRO_0000123424

Regions

Domain1 – 785785Myosin head-like
Domain786 – 81530IQ
Nucleotide binding178 – 1858ATP Potential
Region661 – 68323Actin-binding By similarity
Region762 – 77615Actin-binding By similarity
Region1935 – 197238C-terminal
Coiled coil844 – 19341091 Potential

Amino acid modifications

Modified residue81Phosphoserine By similarity
Modified residue1291N6,N6,N6-trimethyllysine Potential
Modified residue19541Phosphoserine Ref.12

Natural variations

Alternative sequence2111T → TQGPSFAY in isoform 2 and isoform 3.
VSP_043017
Alternative sequence1930 – 197243RGNET…TKASE → GPPPQETSQ in isoform 3 and isoform 4.
VSP_043018
Natural variant11041A → T.
Corresponds to variant rs34263860 [ dbSNP | Ensembl ].
VAR_050205
Natural variant12341A → T.
Corresponds to variant rs16967494 [ dbSNP | Ensembl ].
VAR_030239
Natural variant1241 – 126424Missing in AAT4.
VAR_031734
Natural variant12891V → A.
Corresponds to variant rs16967510 [ dbSNP | Ensembl ].
VAR_030240
Natural variant13101V → M.
Corresponds to variant rs7196804 [ dbSNP | Ensembl ].
VAR_030241
Natural variant15081M → V.
Corresponds to variant rs35176378 [ dbSNP | Ensembl ].
VAR_050206
Natural variant17581R → Q in AAT4. Ref.14
VAR_031735

Experimental info

Sequence conflict887 – 8893EEK → NSE in D10667. Ref.9
Sequence conflict15581T → S in D10667. Ref.9
Sequence conflict1610 – 16112KQ → NE in D10667. Ref.9
Sequence conflict17861A → S in CAA49154. Ref.10
Sequence conflict19581T → L in D10667. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SM-A) [UniParc].

Last modified April 27, 2001. Version 3.
Checksum: 67665BB2AECE1277

FASTA1,972227,339
        10         20         30         40         50         60 
MAQKGQLSDD EKFLFVDKNF INSPVAQADW AAKRLVWVPS EKQGFEAASI KEEKGDEVVV 

        70         80         90        100        110        120 
ELVENGKKVT VGKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLRERYF SGLIYTYSGL 

       130        140        150        160        170        180 
FCVVVNPYKH LPIYSEKIVD MYKGKKRHEM PPHIYAIADT AYRSMLQDRE DQSILCTGES 

       190        200        210        220        230        240 
GAGKTENTKK VIQYLAVVAS SHKGKKDTSI TGELEKQLLQ ANPILEAFGN AKTVKNDNSS 

       250        260        270        280        290        300 
RFGKFIRINF DVTGYIVGAN IETYLLEKSR AIRQARDERT FHIFYYMIAG AKEKMRSDLL 

       310        320        330        340        350        360 
LEGFNNYTFL SNGFVPIPAA QDDEMFQETV EAMAIMGFSE EEQLSILKVV SSVLQLGNIV 

       370        380        390        400        410        420 
FKKERNTDQA SMPDNTAAQK VCHLMGINVT DFTRSILTPR IKVGRDVVQK AQTKEQADFA 

       430        440        450        460        470        480 
VEALAKATYE RLFRWILTRV NKALDKTHRQ GASFLGILDI AGFEIFEVNS FEQLCINYTN 

       490        500        510        520        530        540 
EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCIE LIERPNNPPG VLALLDEECW 

       550        560        570        580        590        600 
FPKATDKSFV EKLCTEQGSH PKFQKPKQLK DKTEFSIIHY AGKVDYNASA WLTKNMDPLN 

       610        620        630        640        650        660 
DNVTSLLNAS SDKFVADLWK DVDRIVGLDQ MAKMTESSLP SASKTKKGMF RTVGQLYKEQ 

       670        680        690        700        710        720 
LGKLMTTLRN TTPNFVRCII PNHEKRSGKL DAFLVLEQLR CNGVLEGIRI CRQGFPNRIV 

       730        740        750        760        770        780 
FQEFRQRYEI LAANAIPKGF MDGKQACILM IKALELDPNL YRIGQSKIFF RTGVLAHLEE 

       790        800        810        820        830        840 
ERDLKITDVI MAFQAMCRGY LARKAFAKRQ QQLTAMKVIQ RNCAAYLKLR NWQWWRLFTK 

       850        860        870        880        890        900 
VKPLLQVTRQ EEEMQAKEDE LQKTKERQQK AENELKELEQ KHSQLTEEKN LLQEQLQAET 

       910        920        930        940        950        960 
ELYAEAEEMR VRLAAKKQEL EEILHEMEAR LEEEEDRGQQ LQAERKKMAQ QMLDLEEQLE 

       970        980        990       1000       1010       1020 
EEEAARQKLQ LEKVTAEAKI KKLEDEILVM DDQNNKLSKE RKLLEERISD LTTNLAEEEE 

      1030       1040       1050       1060       1070       1080 
KAKNLTKLKN KHESMISELE VRLKKEEKSR QELEKLKRKL EGDASDFHEQ IADLQAQIAE 

      1090       1100       1110       1120       1130       1140 
LKMQLAKKEE ELQAALARLD DEIAQKNNAL KKIRELEGHI SDLQEDLDSE RAARNKAEKQ 

      1150       1160       1170       1180       1190       1200 
KRDLGEELEA LKTELEDTLD STATQQELRA KREQEVTVLK KALDEETRSH EAQVQEMRQK 

      1210       1220       1230       1240       1250       1260 
HAQAVEELTE QLEQFKRAKA NLDKNKQTLE KENADLAGEL RVLGQAKQEV EHKKKKLEAQ 

      1270       1280       1290       1300       1310       1320 
VQELQSKCSD GERARAELND KVHKLQNEVE SVTGMLNEAE GKAIKLAKDV ASLSSQLQDT 

      1330       1340       1350       1360       1370       1380 
QELLQEETRQ KLNVSTKLRQ LEEERNSLQD QLDEEMEAKQ NLERHISTLN IQLSDSKKKL 

      1390       1400       1410       1420       1430       1440 
QDFASTVEAL EEGKKRFQKE IENLTQQYEE KAAAYDKLEK TKNRLQQELD DLVVDLDNQR 

      1450       1460       1470       1480       1490       1500 
QLVSNLEKKQ RKFDQLLAEE KNISSKYADE RDRAEAEARE KETKALSLAR ALEEALEAKE 

      1510       1520       1530       1540       1550       1560 
ELERTNKMLK AEMEDLVSSK DDVGKNVHEL EKSKRALETQ MEEMKTQLEE LEDELQATED 

      1570       1580       1590       1600       1610       1620 
AKLRLEVNMQ ALKGQFERDL QARDEQNEEK RRQLQRQLHE YETELEDERK QRALAAAAKK 

      1630       1640       1650       1660       1670       1680 
KLEGDLKDLE LQADSAIKGR EEAIKQLRKL QAQMKDFQRE LEDARASRDE IFATAKENEK 

      1690       1700       1710       1720       1730       1740 
KAKSLEADLM QLQEDLAAAE RARKQADLEK EELAEELASS LSGRNALQDE KRRLEARIAQ 

      1750       1760       1770       1780       1790       1800 
LEEELEEEQG NMEAMSDRVR KATQQAEQLS NELATERSTA QKNESARQQL ERQNKELRSK 

      1810       1820       1830       1840       1850       1860 
LHEMEGAVKS KFKSTIAALE AKIAQLEEQV EQEAREKQAA TKSLKQKDKK LKEILLQVED 

      1870       1880       1890       1900       1910       1920 
ERKMAEQYKE QAEKGNARVK QLKRQLEEAE EESQRINANR RKLQRELDEA TESNEAMGRE 

      1930       1940       1950       1960       1970 
VNALKSKLRR GNETSFVPSR RSGGRRVIEN ADGSEEETDT RDADFNGTKA SE 

« Hide

Isoform 2 (SM-B1) [UniParc].

Checksum: 9B70CDC6279DC694
Show »

FASTA1,979228,090
Isoform 3 (SM-B2) [UniParc].

Checksum: 0FA4E1636B68B8AC
Show »

FASTA1,945224,328
Isoform 4 [UniParc].

Checksum: 61D4A502A155BEC0
Show »

FASTA1,938223,577

References

« Hide 'large scale' references
[1]"(+)Insert smooth muscle myosin heavy chain (SM-B) isoform expression in human tissues."
Leguillette R., Gil F.R., Zitouni N., Lajoie-Kadoch S., Sobieszek A., Lauzon A.M.
Am. J. Physiol. 289:C1277-C1285(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY.
[2]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]Nagase T., Kikuno R., Yamakawa H., Ohara O.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[5]NHLBI resequencing and genotyping service (RS&G)
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
Tissue: Colon.
[9]"Human smooth muscle myosin heavy chain gene mapped to chromosomal region 16q12."
Matsuoka R., Yoshida M.C., Furutani Y., Imamura S., Kanda N., Yanagisawa M., Masaki T., Takao A.
Am. J. Med. Genet. 46:61-67(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 885-1972 (ISOFORM 1/2).
[10]Okajima K.
Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1093-1972 (ISOFORM 1/2).
Tissue: Hippocampus.
[11]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[12]"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-1954, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[13]"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].
[14]"Mutations in myosin heavy chain 11 cause a syndrome associating thoracic aortic aneurysm/aortic dissection and patent ductus arteriosus."
Zhu L., Vranckx R., Khau Van Kien P., Lalande A., Boisset N., Mathieu F., Wegman M., Glancy L., Gasc J.-M., Brunotte F., Bruneval P., Wolf J.-E., Michel J.-B., Jeunemaitre X.
Nat. Genet. 38:343-349(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AAT4 1241-ARG--LEU-1264 DEL AND GLN-1758.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY520816 mRNA. Translation: AAS98910.1.
AY520817 mRNA. Translation: AAS98911.1.
AF001548 Genomic DNA. Translation: AAC31665.1.
U91323 Genomic DNA. Translation: AAC35212.1.
AB020673 mRNA. Translation: BAA74889.2. Different initiation.
GU143399 Genomic DNA. Translation: ACZ58373.1.
GU143400 Genomic DNA. Translation: ACZ58374.1.
AC024120 Genomic DNA. No translation available.
AC026401 Genomic DNA. No translation available.
AC130651 Genomic DNA. No translation available.
CH471226 Genomic DNA. Translation: EAW53924.1.
CH471226 Genomic DNA. Translation: EAW53926.1.
BC101677 mRNA. Translation: AAI01678.1.
BC104906 mRNA. Translation: AAI04907.1.
BC143364 mRNA. Translation: AAI43365.1.
D10667 mRNA. No translation available.
X69292 mRNA. Translation: CAA49154.1.
RefSeqNP_001035202.1. NM_001040113.1.
NP_001035203.1. NM_001040114.1.
NP_002465.1. NM_002474.2.
NP_074035.1. NM_022844.2.
UniGeneHs.460109.

3D structure databases

ProteinModelPortalP35749.
SMRP35749. Positions 7-904.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110714. 16 interactions.
DIPDIP-47268N.
IntActP35749. 8 interactions.
MINTMINT-2802946.
STRING9606.ENSP00000379616.

PTM databases

PhosphoSiteP35749.

Polymorphism databases

DMDM13432177.

Proteomic databases

PaxDbP35749.
PRIDEP35749.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300036; ENSP00000300036; ENSG00000133392. [P35749-1]
ENST00000396324; ENSP00000379616; ENSG00000133392. [P35749-2]
ENST00000452625; ENSP00000407821; ENSG00000133392. [P35749-3]
ENST00000576790; ENSP00000458731; ENSG00000133392. [P35749-4]
GeneID4629.
KEGGhsa:4629.
UCSCuc002ddv.3. human. [P35749-3]
uc002ddw.3. human. [P35749-4]
uc002ddx.3. human. [P35749-2]
uc002ddy.3. human. [P35749-1]

Organism-specific databases

CTD4629.
GeneCardsGC16M015704.
HGNCHGNC:7569. MYH11.
HPACAB002302.
HPA014539.
HPA015310.
MIM132900. phenotype.
160745. gene.
neXtProtNX_P35749.
Orphanet98829. Acute myeloid leukemia with abnormal bone marrow eosinophils inv(16)(p13q22) or t(16;16)(p13;q22).
229. Familial aortic dissection.
91387. Familial thoracic aortic aneurysm and aortic dissection.
PharmGKBPA31367.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5022.
HOGENOMHOG000173958.
HOVERGENHBG004704.
KOK10352.
OMAFVDKNFV.
OrthoDBEOG71CFK3.
PhylomeDBP35749.
TreeFamTF333601.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_17044. Muscle contraction.

Gene expression databases

ArrayExpressP35749.
BgeeP35749.
CleanExHS_MYH11.
GenevestigatorP35749.

Family and domain databases

Gene3D4.10.270.10. 1 hit.
InterProIPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR008989. Myosin_S1_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50096. IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYH11. human.
GeneWikiMYH11.
GenomeRNAi4629.
NextBio17818.
PROP35749.
SOURCESearch...

Entry information

Entry nameMYH11_HUMAN
AccessionPrimary (citable) accession number: P35749
Secondary accession number(s): D2JYH7 expand/collapse secondary AC list , O00396, O94944, P78422, Q3MIV8, Q3MNF0, Q3MNF1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: April 27, 2001
Last modified: April 16, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

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SIMILARITY comments

Index of protein domains and families

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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