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Q8VIM5 (MYCD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myocardin
Alternative name(s):
Basic SAP coiled-coil transcription activator 2
SRF cofactor protein
Gene names
Name:Myocd
Synonyms:Bsac2, Mycd, Srfcp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length935 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 and differentiation of the smooth muscle cell lineage (myogenesis). Isoform 1 mediates the cardiac transcription factor MEF2C-dependent transcription. Isoform 1 and isoform 3 are more active than isoform 2 and isoform 4 in stimulating cardiac muscle promoters. Ref.1 Ref.5 Ref.8 Ref.11 Ref.13

Subunit structure

Homodimer. Interacts with MLLT7/FOXO4 By similarity. Interacts with SRF, its association does not depend on specific DNA sequences for ternary complex formation. Interacts (via C-terminal) with EP300 (via CREB-binding domain). Interacts with HDAC4 and HDAC5. Interacts with MEF2C. Ref.1 Ref.8 Ref.10 Ref.11

Subcellular location

Nucleus speckle. Note: Nuclear, with a punctate intranuclear pattern with exclusion from nuclei. Ref.1 Ref.10

Tissue specificity

Expressed in heart, aorta, and in smooth muscle cell-containing tissues: stomach, bladder and uterus. Isoform 1 and isoform 3 are predominantly expressed in cardiac muscle whereas isoform 4 and isoform 5 are predominantly expressed in SMC-rich tissues. Isoform 3 is the most abundant isoform inthe heart from embryo to adult. Ref.1 Ref.3 Ref.5 Ref.8 Ref.13

Developmental stage

Detected in the cardiac crescent at 7.75 dpc and in the linear heart tube at 8.0 dpc and the developing atrial and aortic ventricular chambers until birth. Also detected in a subset of vascular and visceral smooth muscle cells: aortic arch arteries at 9.5 dpc; walls of the esophagus, dorsal aorta, pulmonary outflow tract, lung, gut, stomach, small intestine, bladder, and the head mesenchyme at 13.5 dpc until birth. Not detected in skeletal muscle cells. Ref.1 Ref.5

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.

Post-translational modification

Phosphorylation regulates negatively transcriptional activity.

Sequence similarities

Contains 3 RPEL repeats.

Contains 1 SAP domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell differentiation

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

cardiac ventricle development

Inferred from mutant phenotype PubMed 21357509. Source: MGI

cell growth involved in cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

cellular component maintenance

Inferred from mutant phenotype PubMed 19850880. Source: MGI

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

digestive tract development

Inferred from mutant phenotype PubMed 21357509. Source: MGI

ductus arteriosus closure

Inferred from mutant phenotype PubMed 18188448. Source: MGI

heart development

Inferred from mutant phenotype Ref.1. Source: MGI

hepatic stellate cell activation

Inferred from electronic annotation. Source: Ensembl

lung alveolus development

Inferred from mutant phenotype PubMed 21357509. Source: MGI

muscle cell differentiation

Inferred from mutant phenotype PubMed 12867591Ref.3. Source: MGI

negative regulation of cardiac muscle cell apoptotic process

Inferred from mutant phenotype PubMed 19850880. Source: MGI

negative regulation of myotube differentiation

Inferred from mutant phenotype PubMed 17940050. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction Ref.10PubMed 17940050. Source: MGI

positive regulation of DNA binding

Inferred from genetic interaction PubMed 19342595. Source: MGI

positive regulation of cardiac muscle cell differentiation

Inferred from electronic annotation. Source: InterPro

positive regulation of cardiac vascular smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from direct assay Ref.1. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.5PubMed 15798203Ref.11PubMed 17030628PubMed 17940050PubMed 18945672. Source: MGI

positive regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15798203. Source: MGI

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 16224064. Source: BHF-UCL

regulation of cell growth by extracellular stimulus

Inferred from direct assay Ref.1. Source: MGI

regulation of histone acetylation

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of myoblast differentiation

Inferred from mutant phenotype Ref.5. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.3. Source: MGI

smooth muscle cell differentiation

Inferred from mutant phenotype PubMed 18188448PubMed 21357509. Source: MGI

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: GOC

urinary bladder development

Inferred from mutant phenotype PubMed 21357509. Source: MGI

uterus development

Inferred from mutant phenotype PubMed 21357509. Source: MGI

vasculogenesis

Inferred from mutant phenotype PubMed 12867591. Source: MGI

ventricular cardiac muscle cell differentiation

Inferred from mutant phenotype PubMed 21357509. Source: MGI

   Cellular_componentSRF-myogenin-E12 complex

Inferred by curator Ref.1. Source: BHF-UCL

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionR-SMAD binding

Inferred from physical interaction PubMed 16224064. Source: BHF-UCL

RNA polymerase II transcription factor binding transcription factor activity

Inferred from direct assay Ref.1. Source: BHF-UCL

histone acetyltransferase binding

Inferred from physical interaction Ref.10. Source: MGI

histone deacetylase binding

Inferred from physical interaction Ref.10. Source: MGI

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VIM5-1)

Also known as: MYOCD-v2;

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: Q8VIM5-2)

Also known as: BSAC2A; Myocardin A; MYOCD-v5;

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: Missing.
     683-683: Q → QNSGAHEGHSSSFSSPASSLHQPFSGTQADSSHSAGLNPCPKSPSIHPK
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8VIM5-3)

Also known as: =Myocardin A; MYOCD-v1;

The sequence of this isoform differs from the canonical sequence as follows:
     683-683: Q → QNSGAHEGHSSSFSSPASSLHQPFSGTQADSSHSAGLNPCPKSPSIHPK
Isoform 4 (identifier: Q8VIM5-4)

Also known as: MYOCD-v3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
     683-683: Q → QNSGAHEGHSSSFSSPASSLHQPFSGTQADSSHSAGLNPCPKSPSIHPK
Isoform 5 (identifier: Q8VIM5-5)

Also known as: MYOCD-v4;

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 935935Myocardin
PRO_0000126632

Regions

Repeat18 – 4326RPEL 1
Repeat62 – 8726RPEL 2
Repeat106 – 13126RPEL 3
Domain380 – 41435SAP
Region153 – 20149HDAC5-binding
Coiled coil287 – 32236 Potential
Coiled coil519 – 56345 Potential
Motif12 – 2716MEF2C-binding
Compositional bias287 – 32034Gln-rich
Compositional bias300 – 32021Poly-Gln

Amino acid modifications

Modified residue4541Phosphoserine; by GSK3-beta Ref.9
Modified residue4581Phosphoserine; by GSK3-beta Ref.9
Modified residue4621Phosphoserine; by GSK3-beta Ref.9
Modified residue4661Phosphoserine; by GSK3-beta
Modified residue6241Phosphoserine; by GSK3-beta Ref.9
Modified residue6281Phosphoserine; by GSK3-beta Ref.9
Modified residue6321Phosphoserine; by GSK3-beta Ref.9
Modified residue6361Phosphoserine; by GSK3-beta Ref.9
Modified residue8121Phosphoserine; by MAPK1 AND MAPK3 Ref.12
Modified residue8591Phosphoserine; by MAPK1 and MAPK3 Ref.12
Modified residue8661Phosphoserine; by MAPK1 and MAPK3 Ref.12
Modified residue8931Phosphothreonine; by MAPK1 and MAPK3 Ref.12

Natural variations

Alternative sequence1 – 128128Missing in isoform 2.
VSP_007662
Alternative sequence1 – 7979Missing in isoform 4 and isoform 5.
VSP_041684
Alternative sequence6831Q → QNSGAHEGHSSSFSSPASSL HQPFSGTQADSSHSAGLNPC PKSPSIHPK in isoform 2, isoform 3 and isoform 4.
VSP_007663

Experimental info

Mutagenesis387 – 3893ELR → PSF: Activation of ANF promoter abolished, no effect on SM22 promoter. Ref.1
Mutagenesis408 – 4103DRL → PGH: Activation of ANF promoter abolished, no effect on SM22 promoter. Ref.1
Mutagenesis8121S → A: No effect on SRF activation. No effect on SRF activation, on interaction with EP300 and on SM-promoter activation; when associated with A-859; A-866 and A-893. Ref.12
Mutagenesis8121S → D: No effect on SRF activation. Impairs SRF activation, reduces interaction with EP300 and SM-promoter activation; when associated with D-859; D-866 and D-893. Ref.12
Mutagenesis8591S → A: No effect on SRF activation; No effect on SRF activation. No effect on SRF activation, on interaction with EP300 and on SM-promoter activation; when associated with A-812, A-866 and A-893. Ref.12
Mutagenesis8591S → D: No effect on SRF activation. Impairs SRF activation, reduces interaction with EP300 and SM-promoter activation; when associated with D-812; D-866 and D-893. Ref.12
Mutagenesis8661S → A: No effect on SRF activation; No effect on SRF activation, on interaction with EP300 and on SM-promoter activation; when associated with A-812; A-859 and A-893. Ref.12
Mutagenesis8661S → D: No effect on SRF activation. Impairs SRF activation, reduces interaction with EP300 and SM-promoter activation; when associated with D-812; D-859 and D-893. Ref.12
Mutagenesis8931T → A: No effect on SRF activation; No effect on SRF activation, on interaction with EP300 and on SM-specific genes trancription; when associated with A-812; A-859 and A-866. Ref.12
Mutagenesis8931T → D: No effect on SRF activation. Impairs SRF activation, reduces interaction with EP300 and SM-promoter activation; when associated with D-812; D-859 and D-866. Ref.12
Sequence conflict1161P → Q in AAK71683. Ref.1
Sequence conflict7941D → G in AAK71683. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (MYOCD-v2) [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: A8FCFC68A923A5CB

FASTA935101,400
        10         20         30         40         50         60 
MTLLGSEHSL LIRRKFRSVL QLRLQQRRTQ EQLANQGLIP PLKGPTEFHD PRKQLDSAKT 

        70         80         90        100        110        120 
EDSLRRKGRN RSDRASLVTM HILQASTAER SIPTAQMKLK RARLADDLNE KIALRPGPLE 

       130        140        150        160        170        180 
LVEKNILPMD SSVKEAIKGT EVSLSKAADA FAFEDDSSRD GLSPDQARSE DPQGSTGSTP 

       190        200        210        220        230        240 
DIKSTEAPLD TIQDLTPGSE SDKNDAASQP GNQSDPGKQV LGPLSTPIPV HTAVKSKSLG 

       250        260        270        280        290        300 
DSKNRHKKPK DPKPKVKKLK YHQYIPPDQK AEKSPPPMDS AYARLLQQQQ LFLQLQILSQ 

       310        320        330        340        350        360 
QQQQQQQQQQ QQQQQQQQQQ RFSYPGMHQT HLKEPNEQMA RNPNPSSTPL SNTPLSPVKN 

       370        380        390        400        410        420 
SISGQTGVSS LKPGPLPPNL DDLKVSELRQ QLRIRGLPVS GTKTALVDRL RPFQDCAGNP 

       430        440        450        460        470        480 
VPNFGDITTV TFPVTPNTLP SYQSSPTGFY HFGSTSSSPP ISPASSDLSA AGSLPDTFTD 

       490        500        510        520        530        540 
ASPGFGLHAS PVPACTDESL LSSLNGGSGP SEPDGLDSEK DKMLVEKQKV INQLTWKLRQ 

       550        560        570        580        590        600 
EQRQVEELRM QLQKQKSSCS DQKPLPFLAT TIKQEDVSSC PFAPQQASGK GQGHSSDSPP 

       610        620        630        640        650        660 
PACETAQLLP HCVESSGQTH VLSSTFLSPQ CSPQHSPLGG LKSPQHISLP PSPNNHYFLA 

       670        680        690        700        710        720 
SSSGAQRENH GVSSPSSSQG CAQMTGLQSS DKVGPTFSIP SPTFSKSSSA VSDITQPPSY 

       730        740        750        760        770        780 
EDAVKQQMTR SQQMDELLDV LIESGEMPAD AREDHSCLQK IPKIPGSSCS PTAIPPKPSA 

       790        800        810        820        830        840 
SFEQASSGGQ MAFDHYANDS DEHLEVLLNS HSPIGKVSDV TLLKIGSEEP PFDSIMDGFP 

       850        860        870        880        890        900 
GKAAEDLFSA HELLPGPLSP MHAQLSPPSV DSSGLQLSFT ESPWETMEWL DLTPPSSTPG 

       910        920        930 
FSNLTSSGPS IFNIDFLDVT DLNLNSPMDL HLQQW 

« Hide

Isoform 2 (BSAC2A) (Myocardin A) (MYOCD-v5) [UniParc].

Checksum: 73C3AAB62E61DB33
Show »

FASTA85591,592
Isoform 3 (=Myocardin A) (MYOCD-v1) [UniParc].

Checksum: 7640D2863F9DB517
Show »

FASTA983106,223
Isoform 4 (MYOCD-v3) [UniParc].

Checksum: 535A0D43433EEDD7
Show »

FASTA90497,066
Isoform 5 (MYOCD-v4) [UniParc].

Checksum: D2243E5464F1297D
Show »

FASTA85692,243

References

« Hide 'large scale' references
[1]"Activation of cardiac gene expression by myocardin, a transcriptional cofactor for serum response factor."
Wang D.-Z., Chang P.S., Wang Z., Sutherland L., Richardson J.A., Small E., Krieg P.A., Olson E.N.
Cell 105:851-862(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH SRF, MUTAGENESIS OF 387-GLU--ARG-389 AND 408-ASP--LEU-410.
Tissue: Heart.
[2]"Potentiation of serum response factor activity by a family of myocardin-related transcription factors."
Wang D.-Z., Li S., Hockemeyer D., Sutherland L., Wang Z., Schratt G., Richardson J.A., Nordheim A., Olson E.N.
Proc. Natl. Acad. Sci. U.S.A. 99:14855-14860(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION TO 1-128.
[3]"Myocardin expression is regulated by Nkx2.5, and its function is required for cardiomyogenesis."
Ueyama T., Kasahara H., Ishiwata T., Nie Q., Izumo S.
Mol. Cell. Biol. 23:9222-9232(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
Strain: NIH Swiss.
[4]"An alternative splicing form of myocardin (BSAC2), myocardin A (BSAC2A)."
Sawada T., Okazaki T., Nakano H.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: C57BL/6.
Tissue: Heart.
[5]"Myocardin is a critical serum response factor cofactor in the transcriptional program regulating smooth muscle cell differentiation."
Du K.L., Ip H.S., Li J., Chen M., Dandre F., Yu W., Lu M.M., Owens G.K., Parmacek M.S.
Mol. Cell. Biol. 23:2425-2437(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[6]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Embryonic heart.
[7]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[8]"Myocardin is a key regulator of CArG-dependent transcription of multiple smooth muscle marker genes."
Yoshida T., Sinha S., Dandre F., Wamhoff B.R., Hoofnagle M.H., Kremer B.E., Wang D.-Z., Olson E.N., Owens G.K.
Circ. Res. 92:856-864(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH SRF.
[9]"Glycogen synthase kinase 3beta inhibits myocardin-dependent transcription and hypertrophy induction through site-specific phosphorylation."
Badorff C., Seeger F.H., Zeiher A.M., Dimmeler S.
Circ. Res. 97:645-654(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-454; SER-458; SER-462; SER-466: SER-624; SER-628; SER-632 AND SER-636.
[10]"Modulation of smooth muscle gene expression by association of histone acetyltransferases and deacetylases with myocardin."
Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A., Wang D.Z., Olson E.N.
Mol. Cell. Biol. 25:364-376(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EP300; HDAC4 AND HDAC5.
[11]"Coactivation of MEF2 by the SAP domain proteins myocardin and MASTR."
Creemers E.E., Sutherland L.B., Oh J., Barbosa A.C., Olson E.N.
Mol. Cell 23:83-96(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 2 AND 4), INTERACTION WITH MEF2C, FUNCTION.
[12]"Phosphorylation of myocardin by extracellular signal-regulated kinase."
Taurin S., Sandbo N., Yau D.M., Sethakorn N., Kach J., Dulin N.O.
J. Biol. Chem. 284:33789-33794(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-812; SER-859; SER-866 AND THR-893, MUTAGENESIS OF SER-812; SER-859; SER-866 AND THR-893.
[13]"Expression and functional activity of four myocardin isoforms."
Imamura M., Long X., Nanda V., Miano J.M.
Gene 464:1-10(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5), TISSUE SPECIFICITY OF ISOFORMS, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF384055 mRNA. Translation: AAK71683.2.
AY303755 mRNA. Translation: AAQ63841.1.
AF437877 mRNA. Translation: AAL30892.1.
AK084700 mRNA. Translation: BAC39258.1.
AK142216 mRNA. Translation: BAE24980.1.
AL669846 Genomic DNA. Translation: CAI25017.1.
RefSeqNP_660118.3. NM_145136.4.
NP_666498.2. NM_146386.3.
XP_006532880.1. XM_006532817.1.
UniGeneMm.32257.

3D structure databases

ProteinModelPortalQ8VIM5.
SMRQ8VIM5. Positions 17-129, 372-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229522. 15 interactions.
DIPDIP-29754N.

PTM databases

PhosphoSiteQ8VIM5.

Proteomic databases

PaxDbQ8VIM5.
PRIDEQ8VIM5.

Protocols and materials databases

DNASU214384.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000101042; ENSMUSP00000098603; ENSMUSG00000020542. [Q8VIM5-2]
ENSMUST00000102635; ENSMUSP00000099695; ENSMUSG00000020542. [Q8VIM5-1]
ENSMUST00000108695; ENSMUSP00000104335; ENSMUSG00000020542. [Q8VIM5-3]
GeneID214384.
KEGGmmu:214384.
UCSCuc007jky.2. mouse. [Q8VIM5-3]
uc007jkz.2. mouse. [Q8VIM5-1]

Organism-specific databases

CTD93649.
MGIMGI:2137495. Myocd.

Phylogenomic databases

eggNOGNOG79803.
GeneTreeENSGT00530000063195.
HOGENOMHOG000038001.
HOVERGENHBG036493.
InParanoidQ6W8X1.
OMASFTESPW.
OrthoDBEOG7VMP4N.
TreeFamTF326024.

Gene expression databases

ArrayExpressQ8VIM5.
BgeeQ8VIM5.
CleanExMM_MYOCD.
GenevestigatorQ8VIM5.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
InterProIPR028721. MYOCD.
IPR004018. RPEL_repeat.
IPR003034. SAP_dom.
[Graphical view]
PANTHERPTHR22793:SF4. PTHR22793:SF4. 1 hit.
PfamPF02755. RPEL. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTSM00707. RPEL. 3 hits.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS51073. RPEL. 3 hits.
PS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio374288.
PROQ8VIM5.
SOURCESearch...

Entry information

Entry nameMYCD_MOUSE
AccessionPrimary (citable) accession number: Q8VIM5
Secondary accession number(s): Q5SS65 expand/collapse secondary AC list , Q6W8X1, Q8C3W6, Q8VIL4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot