Q8IZQ8 · MYCD_HUMAN
- ProteinMyocardin
- GeneMYOCD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids938 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Smooth muscle cells (SM) and cardiac muscle cells-specific transcriptional factor which uses the canonical single or multiple CArG boxes DNA sequence. Acts as a cofactor of serum response factor (SRF) with the potential to modulate SRF-target genes. Plays a crucial role in cardiogenesis, urinary bladder development, and differentiation of the smooth muscle cell lineage (myogenesis) (By similarity).
Positively regulates the transcription of genes involved in vascular smooth muscle contraction (By similarity).
Positively regulates the transcription of genes involved in vascular smooth muscle contraction (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMyocardin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8IZQ8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Megabladder, congenital (MGBL)
- Note
- DescriptionAn autosomal dominant congenital anomaly characterized by a massively dilated urinary bladder with disrupted smooth muscle in the bladder wall. MGBL is a sex-limited trait with 95% male predominance, and incomplete penetrance. Affected males frequently die in utero.
- See alsoMIM:618719
Natural variants in MGBL
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_083482 | 115-938 | missing | in MGBL; loss of function in transcriptional activation | |
VAR_083483 | 530 | E>G | in MGBL; uncertain significance; decreased function in transcriptional activation; dbSNP:rs1597809206 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_083482 | 115-938 | in MGBL; loss of function in transcriptional activation | |||
Sequence: Missing | ||||||
Natural variant | VAR_083483 | 530 | in MGBL; uncertain significance; decreased function in transcriptional activation; dbSNP:rs1597809206 | |||
Sequence: E → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,370 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000126631 | 1-938 | UniProt | Myocardin | |||
Sequence: MTLLGSEHSLLIRSKFRSVLQLRLQQRRTQEQLANQGIIPPLKRPAEFHEQRKHLDSDKAKNSLKRKARNRCNSADLVNMHILQASTAERSIPTAQMKLKRARLADDLNEKIALRPGPLELVEKNILPVDSAVKEAIKGNQVSFSKSTDAFAFEEDSSSDGLSPDQTRSEDPQNSAGSPPDAKASDTPSTGSLGTNQDLASGSENDRNDSASQPSHQSDAGKQGLGPPSTPIAVHAAVKSKSLGDSKNRHKKPKDPKPKVKKLKYHQYIPPDQKAEKSPPPMDSAYARLLQQQQLFLQLQILSQQQQQQQHRFSYLGMHQAQLKEPNEQMVRNPNSSSTPLSNTPLSPVKNSFSGQTGVSSFKPGPLPPNLDDLKVSELRQQLRIRGLPVSGTKTALMDRLRPFQDCSGNPVPNFGDITTVTFPVTPNTLPNYQSSSSTSALSNGFYHFGSTSSSPPISPASSDLSVAGSLPDTFNDASPSFGLHPSPVHVCTEESLMSSLNGGSVPSELDGLDSEKDKMLVEKQKVINELTWKLQQEQRQVEELRMQLQKQKRNNCSEKKPLPFLAASIKQEEAVSSCPFASQVPVKRQSSSSECHPPACEAAQLQPLGNAHCVESSDQTNVLSSTFLSPQCSPQHSPLGAVKSPQHISLPPSPNNPHFLPSSSGAQGEGHRVSSPISSQVCTAQMAGLHSSDKVGPKFSIPSPTFSKSSSAISEVTQPPSYEDAVKQQMTRSQQMDELLDVLIESGEMPADAREDHSCLQKVPKIPRSSRSPTAVLTKPSASFEQASSGSQIPFDPYATDSDEHLEVLLNSQSPLGKMSDVTLLKIGSEEPHFDGIMDGFSGKAAEDLFNAHEILPGPLSPMQTQFSPSSVDSNGLQLSFTESPWETMEWLDLTPPNSTPGFSALTTSSPSIFNIDFLDVTDLNLNSSMDLHLQQW | |||||||
Modified residue (large scale data) | 347 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 451 | UniProt | Phosphoserine; by GSK3-beta | ||||
Sequence: S | |||||||
Modified residue | 455 | UniProt | Phosphoserine; by GSK3-beta | ||||
Sequence: S | |||||||
Modified residue | 459 | UniProt | Phosphoserine; by GSK3-beta | ||||
Sequence: S | |||||||
Modified residue | 463 | UniProt | Phosphoserine; by GSK3-beta | ||||
Sequence: S | |||||||
Modified residue | 626 | UniProt | Phosphoserine; by GSK3-beta | ||||
Sequence: S | |||||||
Modified residue | 630 | UniProt | Phosphoserine; by GSK3-beta | ||||
Sequence: S | |||||||
Modified residue | 634 | UniProt | Phosphoserine; by GSK3-beta | ||||
Sequence: S | |||||||
Modified residue | 638 | UniProt | Phosphoserine; by GSK3-beta | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 704 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 773 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 815 | UniProt | Phosphoserine; by MAPK1 and MAPK3 | ||||
Sequence: S | |||||||
Modified residue | 862 | UniProt | Phosphoserine; by MAPK1 and MAPK3 | ||||
Sequence: S | |||||||
Modified residue | 869 | UniProt | Phosphoserine; by MAPK1 and MAPK3 | ||||
Sequence: S | |||||||
Modified residue | 896 | UniProt | Phosphothreonine; by MAPK1 and MAPK3 | ||||
Sequence: T |
Post-translational modification
Ubiquitinated; by STUB1/CHIP at the C-terminus, leading to its degradation by the proteasome (By similarity).
Phosphorylation by GSK3B is required for STUB1/CHIP-mediated ubiquitination (By similarity).
Phosphorylation by GSK3B is required for STUB1/CHIP-mediated ubiquitination (By similarity).
Phosphorylation negatively regulates the intrinsic myocardin transcriptional activity (By similarity).
Phosphorylated; by GSK3B (By similarity).
Phosphorylated; by GSK3B (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the heart, aorta and bladder (PubMed:12640126, PubMed:20385216).
Expressed in smooth muscle cell-containing tissues: stomach, small intestine, colon, lung, placenta and uterus (PubMed:12640126).
Very faint expression in prostate and skeletal muscle (PubMed:12640126).
Expressed in smooth muscle cell-containing tissues: stomach, small intestine, colon, lung, placenta and uterus (PubMed:12640126).
Very faint expression in prostate and skeletal muscle (PubMed:12640126).
Induction
Up-regulated during end-stage heart failure caused by dilated cardiomyopathy.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer. Interacts with SRF, its association does not depend on specific DNA sequences for ternary complex formation (By similarity).
Interacts with MLLT7/FOXO4. Interacts (via C-terminal) with EP300 (via the CREB-binding domain). Interacts with HDAC4 and HDAC5 (By similarity).
Interacts with MEF2C (By similarity).
Interacts (via C-terminus) with STUB1/CHIP (By similarity).
Interacts with PURB (By similarity).
Interacts with MLLT7/FOXO4. Interacts (via C-terminal) with EP300 (via the CREB-binding domain). Interacts with HDAC4 and HDAC5 (By similarity).
Interacts with MEF2C (By similarity).
Interacts (via C-terminus) with STUB1/CHIP (By similarity).
Interacts with PURB (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8IZQ8 | GOPC Q9HD26 | 4 | EBI-493384, EBI-349832 | |
BINARY | Q8IZQ8 | SRF P11831 | 2 | EBI-493384, EBI-493034 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, repeat, compositional bias, region, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 12-27 | MEF2C-binding | ||||
Sequence: IRSKFRSVLQLRLQQR | ||||||
Repeat | 18-43 | RPEL 1 | ||||
Sequence: SVLQLRLQQRRTQEQLANQGIIPPLK | ||||||
Compositional bias | 48-63 | Basic and acidic residues | ||||
Sequence: FHEQRKHLDSDKAKNS | ||||||
Region | 48-68 | Disordered | ||||
Sequence: FHEQRKHLDSDKAKNSLKRKA | ||||||
Repeat | 62-87 | RPEL 2 | ||||
Sequence: NSLKRKARNRCNSADLVNMHILQAST | ||||||
Repeat | 106-131 | RPEL 3 | ||||
Sequence: DDLNEKIALRPGPLELVEKNILPVDS | ||||||
Region | 153-205 | HDAC5-binding | ||||
Sequence: FEEDSSSDGLSPDQTRSEDPQNSAGSPPDAKASDTPSTGSLGTNQDLASGSEN | ||||||
Compositional bias | 154-224 | Polar residues | ||||
Sequence: EEDSSSDGLSPDQTRSEDPQNSAGSPPDAKASDTPSTGSLGTNQDLASGSENDRNDSASQPSHQSDAGKQG | ||||||
Region | 154-281 | Disordered | ||||
Sequence: EEDSSSDGLSPDQTRSEDPQNSAGSPPDAKASDTPSTGSLGTNQDLASGSENDRNDSASQPSHQSDAGKQGLGPPSTPIAVHAAVKSKSLGDSKNRHKKPKDPKPKVKKLKYHQYIPPDQKAEKSPPP | ||||||
Domain | 371-405 | SAP | ||||
Sequence: LDDLKVSELRQQLRIRGLPVSGTKTALMDRLRPFQ | ||||||
Coiled coil | 516-561 | |||||
Sequence: EKDKMLVEKQKVINELTWKLQQEQRQVEELRMQLQKQKRNNCSEKK | ||||||
Region | 635-678 | Disordered | ||||
Sequence: PQHSPLGAVKSPQHISLPPSPNNPHFLPSSSGAQGEGHRVSSPI | ||||||
Compositional bias | 660-678 | Polar residues | ||||
Sequence: FLPSSSGAQGEGHRVSSPI | ||||||
Region | 693-734 | Disordered | ||||
Sequence: SDKVGPKFSIPSPTFSKSSSAISEVTQPPSYEDAVKQQMTRS | ||||||
Compositional bias | 703-734 | Polar residues | ||||
Sequence: PSPTFSKSSSAISEVTQPPSYEDAVKQQMTRS | ||||||
Region | 717-938 | Required for interaction with and ubiquitination by STUB1 | ||||
Sequence: VTQPPSYEDAVKQQMTRSQQMDELLDVLIESGEMPADAREDHSCLQKVPKIPRSSRSPTAVLTKPSASFEQASSGSQIPFDPYATDSDEHLEVLLNSQSPLGKMSDVTLLKIGSEEPHFDGIMDGFSGKAAEDLFNAHEILPGPLSPMQTQFSPSSVDSNGLQLSFTESPWETMEWLDLTPPNSTPGFSALTTSSPSIFNIDFLDVTDLNLNSSMDLHLQQW |
Domain
The C-terminal region contains a general transcription activation domain. The N-terminal region, comprising a basic and a Gln-rich domain, confers transcriptional potency and specificity by mediating association with the MADS box of SRF. The basic domain may be required for nuclear localization. The SAP domain is important for transactivation and ternary complex formation (By similarity).
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q8IZQ8-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsMyocardin-A
- Length938
- Mass (Da)101,997
- Last updated2003-03-01 v1
- Checksum295F66A02725B0A5
Q8IZQ8-2
- Name2
- SynonymsMyocardin-C
Q8IZQ8-3
- Name3
- SynonymsMyocardin-B
- Differences from canonical
- 686-686: Q → QNSGAHDGHPPSFSPHSSSLHPPFSGAQADSSHGAGGNPCPKSPCVQQK
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_007658 | 1-96 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 48-63 | Basic and acidic residues | ||||
Sequence: FHEQRKHLDSDKAKNS | ||||||
Compositional bias | 154-224 | Polar residues | ||||
Sequence: EEDSSSDGLSPDQTRSEDPQNSAGSPPDAKASDTPSTGSLGTNQDLASGSENDRNDSASQPSHQSDAGKQG | ||||||
Compositional bias | 660-678 | Polar residues | ||||
Sequence: FLPSSSGAQGEGHRVSSPI | ||||||
Alternative sequence | VSP_007659 | 686 | in isoform 2 and isoform 3 | |||
Sequence: Q → QNSGAHDGHPPSFSPHSSSLHPPFSGAQADSSHGAGGNPCPKSPCVQQK | ||||||
Compositional bias | 703-734 | Polar residues | ||||
Sequence: PSPTFSKSSSAISEVTQPPSYEDAVKQQMTRS | ||||||
Alternative sequence | VSP_007660 | 730-732 | in isoform 2 | |||
Sequence: QMT → VTM | ||||||
Alternative sequence | VSP_007661 | 733-938 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF532596 EMBL· GenBank· DDBJ | AAN33040.1 EMBL· GenBank· DDBJ | mRNA | ||
AY764180 EMBL· GenBank· DDBJ | AAV33439.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292885 EMBL· GenBank· DDBJ | BAF85574.1 EMBL· GenBank· DDBJ | mRNA | ||
AK097821 EMBL· GenBank· DDBJ | BAC05177.1 EMBL· GenBank· DDBJ | mRNA | ||
AC005358 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC126307 EMBL· GenBank· DDBJ | AAI26308.1 EMBL· GenBank· DDBJ | mRNA | ||
BC143391 EMBL· GenBank· DDBJ | AAI43392.1 EMBL· GenBank· DDBJ | mRNA |