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P35749

- MYH11_HUMAN

UniProt

P35749 - MYH11_HUMAN

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Protein

Myosin-11

Gene

MYH11

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

Functioni

Muscle contraction.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi178 – 1858ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. motor activity Source: Ensembl
  3. structural constituent of muscle Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: Reactome
  2. cardiac muscle fiber development Source: UniProtKB
  3. elastic fiber assembly Source: UniProtKB
  4. muscle contraction Source: Reactome
  5. skeletal muscle myosin thick filament assembly Source: UniProtKB
  6. smooth muscle contraction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Muscle protein, Myosin

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_20558. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-11
Alternative name(s):
Myosin heavy chain 11
Myosin heavy chain, smooth muscle isoform
SMMHC
Gene namesi
Name:MYH11
Synonyms:KIAA0866
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:7569. MYH11.

Subcellular locationi

Melanosome 1 Publication
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Thick filaments of the myofibrils.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. muscle myosin complex Source: ProtInc
  4. myosin filament Source: UniProtKB-KW
  5. smooth muscle contractile fiber Source: Ensembl
  6. stress fiber Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Thick filament

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving MYH11 is found in acute myeloid leukemia of M4EO subtype. Pericentric inversion inv(16)(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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1241 – 126424Missing in AAT4. 1 Publication
VAR_031734Add
BLAST
Natural varianti1758 – 17581R → Q in AAT4. 1 Publication
VAR_031735

Keywords - Diseasei

Aortic aneurysm, Disease mutation, Proto-oncogene

Organism-specific databases

MIMi132900. phenotype.
Orphaneti98829. 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.
PharmGKBiPA31367.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19721972Myosin-11PRO_0000123424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81PhosphoserineBy similarity
Modified residuei129 – 1291N6,N6,N6-trimethyllysineSequence Analysis
Modified residuei1954 – 19541Phosphoserine1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP35749.
PaxDbiP35749.
PRIDEiP35749.

PTM databases

PhosphoSiteiP35749.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP35749.
CleanExiHS_MYH11.
ExpressionAtlasiP35749. baseline and differential.
GenevestigatoriP35749.

Organism-specific databases

HPAiCAB002302.
HPA014539.
HPA015310.

Interactioni

Subunit structurei

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).

Binary interactionsi

WithEntry#Exp.IntActNotes
MYL12BO149502EBI-1052928,EBI-1642165

Protein-protein interaction databases

BioGridi110714. 24 interactions.
DIPiDIP-47268N.
IntActiP35749. 9 interactions.
MINTiMINT-2802946.
STRINGi9606.ENSP00000379616.

Structurei

3D structure databases

ProteinModelPortaliP35749.
SMRiP35749. Positions 7-904.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 783699Myosin motorAdd
BLAST
Domaini786 – 81530IQPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni661 – 68323Actin-bindingBy similarityAdd
BLAST
Regioni762 – 77615Actin-bindingBy similarityAdd
BLAST
Regioni1935 – 197238C-terminalAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili844 – 19341091Sequence 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.
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).

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.
InParanoidiP35749.
KOiK10352.
OMAiQAKQDVE.
OrthoDBiEOG71CFK3.
PhylomeDBiP35749.
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.
IPR008989. Myosin_S1_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00063. 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]
SUPFAMiSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35749-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAQKGQLSDD EKFLFVDKNF INSPVAQADW AAKRLVWVPS EKQGFEAASI
60 70 80 90 100
KEEKGDEVVV ELVENGKKVT VGKDDIQKMN PPKFSKVEDM AELTCLNEAS
110 120 130 140 150
VLHNLRERYF SGLIYTYSGL FCVVVNPYKH LPIYSEKIVD MYKGKKRHEM
160 170 180 190 200
PPHIYAIADT AYRSMLQDRE DQSILCTGES GAGKTENTKK VIQYLAVVAS
210 220 230 240 250
SHKGKKDTSI TGELEKQLLQ ANPILEAFGN AKTVKNDNSS RFGKFIRINF
260 270 280 290 300
DVTGYIVGAN IETYLLEKSR AIRQARDERT FHIFYYMIAG AKEKMRSDLL
310 320 330 340 350
LEGFNNYTFL SNGFVPIPAA QDDEMFQETV EAMAIMGFSE EEQLSILKVV
360 370 380 390 400
SSVLQLGNIV FKKERNTDQA SMPDNTAAQK VCHLMGINVT DFTRSILTPR
410 420 430 440 450
IKVGRDVVQK AQTKEQADFA VEALAKATYE RLFRWILTRV NKALDKTHRQ
460 470 480 490 500
GASFLGILDI AGFEIFEVNS FEQLCINYTN EKLQQLFNHT MFILEQEEYQ
510 520 530 540 550
REGIEWNFID FGLDLQPCIE LIERPNNPPG VLALLDEECW FPKATDKSFV
560 570 580 590 600
EKLCTEQGSH PKFQKPKQLK DKTEFSIIHY AGKVDYNASA WLTKNMDPLN
610 620 630 640 650
DNVTSLLNAS SDKFVADLWK DVDRIVGLDQ MAKMTESSLP SASKTKKGMF
660 670 680 690 700
RTVGQLYKEQ LGKLMTTLRN TTPNFVRCII PNHEKRSGKL DAFLVLEQLR
710 720 730 740 750
CNGVLEGIRI CRQGFPNRIV FQEFRQRYEI LAANAIPKGF MDGKQACILM
760 770 780 790 800
IKALELDPNL YRIGQSKIFF RTGVLAHLEE ERDLKITDVI MAFQAMCRGY
810 820 830 840 850
LARKAFAKRQ QQLTAMKVIQ RNCAAYLKLR NWQWWRLFTK VKPLLQVTRQ
860 870 880 890 900
EEEMQAKEDE LQKTKERQQK AENELKELEQ KHSQLTEEKN LLQEQLQAET
910 920 930 940 950
ELYAEAEEMR VRLAAKKQEL EEILHEMEAR LEEEEDRGQQ LQAERKKMAQ
960 970 980 990 1000
QMLDLEEQLE EEEAARQKLQ LEKVTAEAKI KKLEDEILVM DDQNNKLSKE
1010 1020 1030 1040 1050
RKLLEERISD LTTNLAEEEE KAKNLTKLKN KHESMISELE VRLKKEEKSR
1060 1070 1080 1090 1100
QELEKLKRKL EGDASDFHEQ IADLQAQIAE LKMQLAKKEE ELQAALARLD
1110 1120 1130 1140 1150
DEIAQKNNAL KKIRELEGHI SDLQEDLDSE RAARNKAEKQ KRDLGEELEA
1160 1170 1180 1190 1200
LKTELEDTLD STATQQELRA KREQEVTVLK KALDEETRSH EAQVQEMRQK
1210 1220 1230 1240 1250
HAQAVEELTE QLEQFKRAKA NLDKNKQTLE KENADLAGEL RVLGQAKQEV
1260 1270 1280 1290 1300
EHKKKKLEAQ VQELQSKCSD GERARAELND KVHKLQNEVE SVTGMLNEAE
1310 1320 1330 1340 1350
GKAIKLAKDV ASLSSQLQDT QELLQEETRQ KLNVSTKLRQ LEEERNSLQD
1360 1370 1380 1390 1400
QLDEEMEAKQ NLERHISTLN IQLSDSKKKL QDFASTVEAL EEGKKRFQKE
1410 1420 1430 1440 1450
IENLTQQYEE KAAAYDKLEK TKNRLQQELD DLVVDLDNQR QLVSNLEKKQ
1460 1470 1480 1490 1500
RKFDQLLAEE KNISSKYADE RDRAEAEARE KETKALSLAR ALEEALEAKE
1510 1520 1530 1540 1550
ELERTNKMLK AEMEDLVSSK DDVGKNVHEL EKSKRALETQ MEEMKTQLEE
1560 1570 1580 1590 1600
LEDELQATED AKLRLEVNMQ ALKGQFERDL QARDEQNEEK RRQLQRQLHE
1610 1620 1630 1640 1650
YETELEDERK QRALAAAAKK KLEGDLKDLE LQADSAIKGR EEAIKQLRKL
1660 1670 1680 1690 1700
QAQMKDFQRE LEDARASRDE IFATAKENEK KAKSLEADLM QLQEDLAAAE
1710 1720 1730 1740 1750
RARKQADLEK EELAEELASS LSGRNALQDE KRRLEARIAQ LEEELEEEQG
1760 1770 1780 1790 1800
NMEAMSDRVR KATQQAEQLS NELATERSTA QKNESARQQL ERQNKELRSK
1810 1820 1830 1840 1850
LHEMEGAVKS KFKSTIAALE AKIAQLEEQV EQEAREKQAA TKSLKQKDKK
1860 1870 1880 1890 1900
LKEILLQVED ERKMAEQYKE QAEKGNARVK QLKRQLEEAE EESQRINANR
1910 1920 1930 1940 1950
RKLQRELDEA TESNEAMGRE VNALKSKLRR GNETSFVPSR RSGGRRVIEN
1960 1970
ADGSEEETDT RDADFNGTKA SE
Length:1,972
Mass (Da):227,339
Last modified:April 27, 2001 - v3
Checksum:i67665BB2AECE1277
GO
Isoform 2 (identifier: P35749-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,979
Mass (Da):228,090
Checksum:i9B70CDC6279DC694
GO
Isoform 3 (identifier: P35749-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,945
Mass (Da):224,328
Checksum:i0FA4E1636B68B8AC
GO
Isoform 4 (identifier: P35749-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1930-1972: RGNETSFVPSRRSGGRRVIENADGSEEETDTRDADFNGTKASE → GPPPQETSQ

Note: No experimental confirmation available.

Show »
Length:1,938
Mass (Da):223,577
Checksum:i61D4A502A155BEC0
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti887 – 8893EEK → NSE in D10667. (PubMed:7684189)Curated
Sequence conflicti1558 – 15581T → S in D10667. (PubMed:7684189)Curated
Sequence conflicti1610 – 16112KQ → NE in D10667. (PubMed:7684189)Curated
Sequence conflicti1786 – 17861A → S in CAA49154. 1 PublicationCurated
Sequence conflicti1958 – 19581T → L in D10667. (PubMed:7684189)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1104 – 11041A → T.
Corresponds to variant rs34263860 [ dbSNP | Ensembl ].
VAR_050205
Natural varianti1234 – 12341A → T.
Corresponds to variant rs16967494 [ dbSNP | Ensembl ].
VAR_030239
Natural varianti1241 – 126424Missing in AAT4. 1 Publication
VAR_031734Add
BLAST
Natural varianti1289 – 12891V → A.
Corresponds to variant rs16967510 [ dbSNP | Ensembl ].
VAR_030240
Natural varianti1310 – 13101V → M.
Corresponds to variant rs7196804 [ dbSNP | Ensembl ].
VAR_030241
Natural varianti1508 – 15081M → V.
Corresponds to variant rs35176378 [ dbSNP | Ensembl ].
VAR_050206
Natural varianti1758 – 17581R → Q in AAT4. 1 Publication
VAR_031735

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei211 – 2111T → TQGPSFAY in isoform 2 and isoform 3. 2 PublicationsVSP_043017
Alternative sequencei1930 – 197243RGNET…TKASE → GPPPQETSQ in isoform 3 and isoform 4. 2 PublicationsVSP_043018Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS10565.1. [P35749-1]
CCDS10566.1. [P35749-4]
CCDS45423.1. [P35749-2]
CCDS45424.1. [P35749-3]
RefSeqiNP_001035202.1. NM_001040113.1. [P35749-3]
NP_001035203.1. NM_001040114.1. [P35749-2]
NP_002465.1. NM_002474.2. [P35749-1]
NP_074035.1. NM_022844.2. [P35749-4]
UniGeneiHs.460109.

Genome annotation databases

EnsembliENST00000300036; ENSP00000300036; ENSG00000133392. [P35749-1]
ENST00000396324; ENSP00000379616; ENSG00000133392. [P35749-2]
ENST00000452625; ENSP00000407821; ENSG00000133392. [P35749-3]
ENST00000576790; ENSP00000458731; ENSG00000133392. [P35749-4]
GeneIDi4629.
KEGGihsa:4629.
UCSCiuc002ddv.3. human. [P35749-3]
uc002ddw.3. human. [P35749-4]
uc002ddx.3. human. [P35749-2]
uc002ddy.3. human. [P35749-1]

Polymorphism databases

DMDMi13432177.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, 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
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 .
CCDSi CCDS10565.1. [P35749-1 ]
CCDS10566.1. [P35749-4 ]
CCDS45423.1. [P35749-2 ]
CCDS45424.1. [P35749-3 ]
RefSeqi NP_001035202.1. NM_001040113.1. [P35749-3 ]
NP_001035203.1. NM_001040114.1. [P35749-2 ]
NP_002465.1. NM_002474.2. [P35749-1 ]
NP_074035.1. NM_022844.2. [P35749-4 ]
UniGenei Hs.460109.

3D structure databases

ProteinModelPortali P35749.
SMRi P35749. Positions 7-904.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110714. 24 interactions.
DIPi DIP-47268N.
IntActi P35749. 9 interactions.
MINTi MINT-2802946.
STRINGi 9606.ENSP00000379616.

PTM databases

PhosphoSitei P35749.

Polymorphism databases

DMDMi 13432177.

Proteomic databases

MaxQBi P35749.
PaxDbi P35749.
PRIDEi P35749.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300036 ; ENSP00000300036 ; ENSG00000133392 . [P35749-1 ]
ENST00000396324 ; ENSP00000379616 ; ENSG00000133392 . [P35749-2 ]
ENST00000452625 ; ENSP00000407821 ; ENSG00000133392 . [P35749-3 ]
ENST00000576790 ; ENSP00000458731 ; ENSG00000133392 . [P35749-4 ]
GeneIDi 4629.
KEGGi hsa:4629.
UCSCi uc002ddv.3. human. [P35749-3 ]
uc002ddw.3. human. [P35749-4 ]
uc002ddx.3. human. [P35749-2 ]
uc002ddy.3. human. [P35749-1 ]

Organism-specific databases

CTDi 4629.
GeneCardsi GC16M015704.
GeneReviewsi MYH11.
HGNCi HGNC:7569. MYH11.
HPAi CAB002302.
HPA014539.
HPA015310.
MIMi 132900. phenotype.
160745. gene.
neXtProti NX_P35749.
Orphaneti 98829. 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.
PharmGKBi PA31367.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5022.
GeneTreei ENSGT00760000118919.
HOGENOMi HOG000173958.
HOVERGENi HBG004704.
InParanoidi P35749.
KOi K10352.
OMAi QAKQDVE.
OrthoDBi EOG71CFK3.
PhylomeDBi P35749.
TreeFami TF333601.

Enzyme and pathway databases

Reactomei REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_20558. Smooth Muscle Contraction.

Miscellaneous databases

ChiTaRSi MYH11. human.
GeneWikii MYH11.
GenomeRNAii 4629.
NextBioi 17818.
PROi P35749.
SOURCEi Search...

Gene expression databases

Bgeei P35749.
CleanExi HS_MYH11.
ExpressionAtlasi P35749. baseline and differential.
Genevestigatori P35749.

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.
IPR008989. Myosin_S1_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami 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 SSF50084. SSF50084. 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. "(+)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. 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.
    , 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. 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. 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.

Entry informationi

Entry nameiMYH11_HUMAN
AccessioniPrimary (citable) accession number: P35749
Secondary accession number(s): D2JYH7
, O00396, O94944, P78422, Q3MIV8, Q3MNF0, Q3MNF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: April 27, 2001
Last modified: October 29, 2014
This is version 158 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3