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Q8K4J6 (MKL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MKL/myocardin-like protein 1
Alternative name(s):
Basic SAP coiled-coil transcription activator
Megakaryoblastic leukemia 1 protein homolog
Myocardin-related transcription factor A
Short name=MRTF-A
Gene names
Name:Mkl1
Synonyms:Bsac
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length964 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional coactivator of serum response factor (SRF) with the potential to modulate SRF target genes. Suppresses TNF-induced cell death by inhibiting activation of caspases; its transcriptional activity is indispensable for the antiapoptotic function. It may up-regulate antiapoptotic molecules, which in turn inhibit caspase activation. Ref.5

Subunit structure

Forms with SCAI and SRF a nuclear ternary complex which binds the CArG consensus motif (CArG box) on DNA via SRF. Some authors (Ref.1) have found contradictory results, they could not demonstrate that it forms a complex with the CArG boxes, even in the presence of SRF. Interacts with ACTB; interaction with ACTB prevents interaction with SCAI. Interacts with MKL2. Ref.5

Subcellular location

Cytoplasm. Nucleus. Note: Binding to globular actin is required to maintain cytoplasmic localization. Nuclear localization is regulated by MICAL2, which mediates depolymerization of nuclear globular actin, promoting retention of MKL1 in the nucleus and subsequent formation of an active complex with SRF By similarity. Ref.5 Ref.6

Tissue specificity

Expressed in heart, brain, spleen, lung, liver, muscle, kidney and testis.

Developmental stage

Detected throughout the embryo at 10.5 dpc; higher expression is found at 13.5 dpc in neural mesenchymal cells, skeletal muscle of the tongue, and epithelial cells of the colon and small intestine; at 15.5 dpc, expression in epithelial cells of lung, kidney, bladder, and colon is also detected.

Domain

The N-terminal region is required for nuclear localization and the C-terminal region mediates transcriptional activity.

The RPEL repeats mediate binding to globular actin.

Sequence similarities

Contains 3 RPEL repeats.

Contains 1 SAP domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   LigandActin-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of apoptotic signaling pathway

Inferred from direct assay Ref.1. Source: MGI

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay Ref.1. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17991879PubMed 18945672. Source: MGI

positive regulation of transcription via serum response element binding

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.1PubMed 15798203. Source: MGI

smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15798203. Source: MGI

nucleus

Inferred from direct assay Ref.1PubMed 15798203. Source: MGI

   Molecular_functionactin binding

Inferred from direct assay PubMed 15798203. Source: MGI

actin monomer binding

Inferred from direct assay Ref.5. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 17991879. Source: MGI

transcription coactivator activity

Inferred from direct assay Ref.5. Source: UniProtKB

transcription regulatory region sequence-specific DNA binding

Inferred from direct assay PubMed 17991879. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACTA1P6813515EBI-8291665,EBI-367540From a different organism.
ACTBP607093EBI-8291665,EBI-353944From a different organism.
KPNA3O005059EBI-8291665,EBI-358297From a different organism.
KPNB1Q149745EBI-8291665,EBI-286758From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8K4J6-1)

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.
Isoform 2 (identifier: Q8K4J6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 964964MKL/myocardin-like protein 1
PRO_0000126626

Regions

Repeat15 – 4026RPEL 1
Repeat59 – 8426RPEL 2
Repeat103 – 12826RPEL 3
Domain385 – 41935SAP
Region1 – 291291Mediates interaction with SCAI and ACTB
Coiled coil552 – 60049 Potential
Compositional bias299 – 32527Gln-rich
Compositional bias712 – 844133Pro-rich

Amino acid modifications

Modified residue411Phosphoserine By similarity
Modified residue4881Phosphothreonine By similarity
Modified residue4921Phosphoserine By similarity

Natural variations

Alternative sequence1 – 3535Missing in isoform 2.
VSP_007652

Experimental info

Sequence conflict531E → Q in BAC31809. Ref.3
Sequence conflict7241S → D in BAC40873. Ref.3
Sequence conflict7281S → F in AAM94258. Ref.1

Secondary structure

............... 964
Helix Strand Turn

Details...

Sequences

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

Last modified June 27, 2003. Version 2.
Checksum: AFAEA328A1860CE5

FASTA964102,546
        10         20         30         40         50         60 
MTLLEPEMLM MAVQSVLQLK LQQRRTREEL VSQGIMPPLK SPAAFHEQRR SLERARTEDY 

        70         80         90        100        110        120 
LKRKIRSRPE RAELVRMHIL EETSAEPSLQ AKQLKLKRAR LADDLNEKIA QRPGPMELVE 

       130        140        150        160        170        180 
KNILPVESSL KEAIIVGQVN YPKVADSSSF DEDSSDALSP EQPASHESQG SVPSPLESRV 

       190        200        210        220        230        240 
SDPLPSATSI SPTQVLSQLP MAPDPGETLF LAEQPPLPPA PLLPPSLANG SIVPTAKPAP 

       250        260        270        280        290        300 
TLIKQSQPKS ASEKSQRSKK AKELKPKVKK LKYHQYIPPD QKQDKGAPAM DSSYAKILQQ 

       310        320        330        340        350        360 
QQLFLQLQIL NQQQQQQQQQ HYNYQAILPA PPKPSAETPG SSAPTPSRSL STSSSPSSGT 

       370        380        390        400        410        420 
PGPSGLARQS STALAAKPGA LPANLDDMKV AELKQELKLR SLPVSGTKTE LIERLRAYQD 

       430        440        450        460        470        480 
QVSPAPGAPK APATTSVLSK AGEVVVAFPA ALLSTGSALV TAGLAPAEMV VATVTSNGMV 

       490        500        510        520        530        540 
KFGSTGSTPP VSPTPSERSL LSTGDENSTP GDAFGEMVTS PLTQLTLQAS PLQIVKEEGA 

       550        560        570        580        590        600 
RAASCCLSPG ARAELEGLDK DQMLQEKDKQ IEELTRMLQQ KQQLVELLRL QLEQQKRAQQ 

       610        620        630        640        650        660 
PAPASSPVKR ESGFSSCQLS CQPQGSAHAF GSGLVVPTTN HGDTQAPAPE SPPVVVKQEA 

       670        680        690        700        710        720 
GPPEPDLAPS SQLLLGSQGT SFLKRVSPPT LVTDSTGTHL ILTVTNKSAD GPGLPAGSPQ 

       730        740        750        760        770        780 
QPLSQPGSPA PGPPAQMDLE HPPQPPFATP TSLLKKEPPG YEETVTQQPK QQENGSSSQH 

       790        800        810        820        830        840 
MDDLFDILIQ SGEISADFKE PPSLPGKEKS PPAAAAYGPP LTPQPSPLSE LPQAAPPPGS 

       850        860        870        880        890        900 
PTLPGRLEDF LESSTGLPLL TSGHEGPEPL SLIDDLHSQM LSSSAILDHP PSPMDTSELH 

       910        920        930        940        950        960 
FAPEPSSGMG LDLAVGHLDS MDWLELSSGG PVLSLAPLST AAPSLFSMDF LDGHDLQLHW 


DSCL 

« Hide

Isoform 2 [UniParc].

Checksum: B13D0985013B6E49
Show »

FASTA92998,463

References

« Hide 'large scale' references
[1]"Identification of a novel transcriptional activator, BSAC, by a functional cloning to inhibit tumor necrosis factor-induced cell death."
Sasazuki T., Sawada Y., Sakon S., Kitamura T., Kishi T., Okazaki T., Katano M., Tanaka M., Watanabe M., Yagita H., Okumura K., Nakano H.
J. Biol. Chem. 277:28853-28860(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Spleen.
[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 2).
Strain: C57BL/6.
[3]"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 2).
Strain: C57BL/6J.
Tissue: Brain cortex.
[4]"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] (ISOFORM 2).
Strain: C57BL/6.
Tissue: Brain.
[5]"SCAI acts as a suppressor of cancer cell invasion through the transcriptional control of beta1-integrin."
Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P., Grosse R.
Nat. Cell Biol. 11:557-568(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ACTB; SCAI AND SRF, SUBCELLULAR LOCATION.
[6]"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL."
Mouilleron S., Guettler S., Langer C.A., Treisman R., McDonald N.Q.
EMBO J. 27:3198-3208(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 54-85 IN COMPLEX WITH G-ACTIN, X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 16-41 IN COMPLEX WITH G-ACTIN, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF385582 mRNA. Translation: AAM94258.1.
AF532597 mRNA. Translation: AAN33041.1.
AK044188 mRNA. Translation: BAC31809.1.
AK089416 mRNA. Translation: BAC40873.1.
BC050941 mRNA. Translation: AAH50941.1.
CCDSCCDS37147.1. [Q8K4J6-1]
CCDS49674.1. [Q8K4J6-2]
RefSeqNP_001076005.1. NM_001082536.1. [Q8K4J6-2]
NP_694629.2. NM_153049.3. [Q8K4J6-1]
UniGeneMm.439814.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V51X-ray2.35E/F16-41[»]
2V52X-ray1.45M54-85[»]
2YJEX-ray3.10M16-142[»]
2YJFX-ray3.50M16-142[»]
ProteinModelPortalQ8K4J6.
SMRQ8K4J6. Positions 14-126, 371-433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230180. 2 interactions.
IntActQ8K4J6. 4 interactions.

PTM databases

PhosphoSiteQ8K4J6.

Proteomic databases

PaxDbQ8K4J6.
PRIDEQ8K4J6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000109579; ENSMUSP00000105207; ENSMUSG00000042292. [Q8K4J6-1]
ENSMUST00000134469; ENSMUSP00000119530; ENSMUSG00000042292. [Q8K4J6-2]
ENSMUST00000149582; ENSMUSP00000117745; ENSMUSG00000042292. [Q8K4J6-2]
GeneID223701.
KEGGmmu:223701.
UCSCuc007wwc.1. mouse. [Q8K4J6-1]

Organism-specific databases

CTD57591.
MGIMGI:2384495. Mkl1.

Phylogenomic databases

eggNOGNOG82832.
GeneTreeENSGT00530000063195.
HOGENOMHOG000038001.
HOVERGENHBG036493.
InParanoidQ642U1.
OMAAQMDLEH.
OrthoDBEOG7FR7G1.
PhylomeDBQ8K4J6.
TreeFamTF326024.

Gene expression databases

ArrayExpressQ8K4J6.
BgeeQ8K4J6.
CleanExMM_MKL1.
GenevestigatorQ8K4J6.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
InterProIPR004018. RPEL_repeat.
IPR003034. SAP_dom.
[Graphical view]
PfamPF02755. RPEL. 3 hits.
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

ChiTaRSMKL1. mouse.
EvolutionaryTraceQ8K4J6.
NextBio376834.
PROQ8K4J6.
SOURCESearch...

Entry information

Entry nameMKL1_MOUSE
AccessionPrimary (citable) accession number: Q8K4J6
Secondary accession number(s): Q642U1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 27, 2003
Last modified: July 9, 2014
This is version 110 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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