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Q8K4J6

- MKL1_MOUSE

UniProt

Q8K4J6 - MKL1_MOUSE

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Protein

MKL/myocardin-like protein 1

Gene
Mkl1, Bsac
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. actin binding Source: MGI
  2. actin monomer binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. sequence-specific DNA binding transcription factor activity Source: MGI
  5. transcription coactivator activity Source: UniProtKB
  6. transcription regulatory region sequence-specific DNA binding Source: MGI

GO - Biological processi

  1. negative regulation of apoptotic signaling pathway Source: MGI
  2. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  3. positive regulation of transcription, DNA-templated Source: MGI
  4. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  5. positive regulation of transcription via serum response element binding Source: UniProtKB
  6. smooth muscle cell differentiation Source: Ensembl
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Mkl1
Synonyms:Bsac
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:2384495. Mkl1.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 964964MKL/myocardin-like protein 1PRO_0000126626Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411Phosphoserine By similarity
Modified residuei488 – 4881Phosphothreonine By similarity
Modified residuei492 – 4921Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8K4J6.
PRIDEiQ8K4J6.

PTM databases

PhosphoSiteiQ8K4J6.

Expressioni

Tissue specificityi

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

Developmental stagei

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.

Gene expression databases

ArrayExpressiQ8K4J6.
BgeeiQ8K4J6.
CleanExiMM_MKL1.
GenevestigatoriQ8K4J6.

Interactioni

Subunit structurei

Forms with SCAI and SRF a nuclear ternary complex which binds the CArG consensus motif (CArG box) on DNA via SRF. Some authors (1 Publication) 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 MKL2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
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.

Protein-protein interaction databases

BioGridi230180. 2 interactions.
IntActiQ8K4J6. 4 interactions.

Structurei

Secondary structure

1
964
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 238
Helixi27 – 326
Beta strandi39 – 413
Helixi59 – 668
Helixi71 – 766
Helixi87 – 11024
Helixi115 – 1206

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V51X-ray2.35E/F16-41[»]
2V52X-ray1.45M54-85[»]
2YJEX-ray3.10M16-142[»]
2YJFX-ray3.50M16-142[»]
ProteinModelPortaliQ8K4J6.
SMRiQ8K4J6. Positions 14-126, 371-433.

Miscellaneous databases

EvolutionaryTraceiQ8K4J6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati15 – 4026RPEL 1Add
BLAST
Repeati59 – 8426RPEL 2Add
BLAST
Repeati103 – 12826RPEL 3Add
BLAST
Domaini385 – 41935SAPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 291291Mediates interaction with SCAI and ACTBAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili552 – 60049 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi299 – 32527Gln-richAdd
BLAST
Compositional biasi712 – 844133Pro-richAdd
BLAST

Domaini

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 similaritiesi

Contains 3 RPEL repeats.
Contains 1 SAP domain.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG82832.
GeneTreeiENSGT00530000063195.
HOGENOMiHOG000038001.
HOVERGENiHBG036493.
InParanoidiQ642U1.
OMAiAQMDLEH.
OrthoDBiEOG7FR7G1.
PhylomeDBiQ8K4J6.
TreeFamiTF326024.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR004018. RPEL_repeat.
IPR003034. SAP_dom.
[Graphical view]
PfamiPF02755. RPEL. 3 hits.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00707. RPEL. 3 hits.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS51073. RPEL. 3 hits.
PS50800. SAP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8K4J6-1) [UniParc]FASTAAdd to Basket

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

MTLLEPEMLM MAVQSVLQLK LQQRRTREEL VSQGIMPPLK SPAAFHEQRR    50
SLERARTEDY LKRKIRSRPE RAELVRMHIL EETSAEPSLQ AKQLKLKRAR 100
LADDLNEKIA QRPGPMELVE KNILPVESSL KEAIIVGQVN YPKVADSSSF 150
DEDSSDALSP EQPASHESQG SVPSPLESRV SDPLPSATSI SPTQVLSQLP 200
MAPDPGETLF LAEQPPLPPA PLLPPSLANG SIVPTAKPAP TLIKQSQPKS 250
ASEKSQRSKK AKELKPKVKK LKYHQYIPPD QKQDKGAPAM DSSYAKILQQ 300
QQLFLQLQIL NQQQQQQQQQ HYNYQAILPA PPKPSAETPG SSAPTPSRSL 350
STSSSPSSGT PGPSGLARQS STALAAKPGA LPANLDDMKV AELKQELKLR 400
SLPVSGTKTE LIERLRAYQD QVSPAPGAPK APATTSVLSK AGEVVVAFPA 450
ALLSTGSALV TAGLAPAEMV VATVTSNGMV KFGSTGSTPP VSPTPSERSL 500
LSTGDENSTP GDAFGEMVTS PLTQLTLQAS PLQIVKEEGA RAASCCLSPG 550
ARAELEGLDK DQMLQEKDKQ IEELTRMLQQ KQQLVELLRL QLEQQKRAQQ 600
PAPASSPVKR ESGFSSCQLS CQPQGSAHAF GSGLVVPTTN HGDTQAPAPE 650
SPPVVVKQEA GPPEPDLAPS SQLLLGSQGT SFLKRVSPPT LVTDSTGTHL 700
ILTVTNKSAD GPGLPAGSPQ QPLSQPGSPA PGPPAQMDLE HPPQPPFATP 750
TSLLKKEPPG YEETVTQQPK QQENGSSSQH MDDLFDILIQ SGEISADFKE 800
PPSLPGKEKS PPAAAAYGPP LTPQPSPLSE LPQAAPPPGS PTLPGRLEDF 850
LESSTGLPLL TSGHEGPEPL SLIDDLHSQM LSSSAILDHP PSPMDTSELH 900
FAPEPSSGMG LDLAVGHLDS MDWLELSSGG PVLSLAPLST AAPSLFSMDF 950
LDGHDLQLHW DSCL 964
Length:964
Mass (Da):102,546
Last modified:June 27, 2003 - v2
Checksum:iAFAEA328A1860CE5
GO
Isoform 2 (identifier: Q8K4J6-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:929
Mass (Da):98,463
Checksum:iB13D0985013B6E49
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3535Missing in isoform 2. VSP_007652Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531E → Q in BAC31809. 1 Publication
Sequence conflicti724 – 7241S → D in BAC40873. 1 Publication
Sequence conflicti728 – 7281S → F in AAM94258. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS37147.1. [Q8K4J6-1]
CCDS49674.1. [Q8K4J6-2]
RefSeqiNP_001076005.1. NM_001082536.1. [Q8K4J6-2]
NP_694629.2. NM_153049.3. [Q8K4J6-1]
UniGeneiMm.439814.

Genome annotation databases

EnsembliENSMUST00000109579; ENSMUSP00000105207; ENSMUSG00000042292. [Q8K4J6-1]
ENSMUST00000134469; ENSMUSP00000119530; ENSMUSG00000042292. [Q8K4J6-2]
ENSMUST00000149582; ENSMUSP00000117745; ENSMUSG00000042292. [Q8K4J6-2]
GeneIDi223701.
KEGGimmu:223701.
UCSCiuc007wwc.1. mouse. [Q8K4J6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS37147.1. [Q8K4J6-1 ]
CCDS49674.1. [Q8K4J6-2 ]
RefSeqi NP_001076005.1. NM_001082536.1. [Q8K4J6-2 ]
NP_694629.2. NM_153049.3. [Q8K4J6-1 ]
UniGenei Mm.439814.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V51 X-ray 2.35 E/F 16-41 [» ]
2V52 X-ray 1.45 M 54-85 [» ]
2YJE X-ray 3.10 M 16-142 [» ]
2YJF X-ray 3.50 M 16-142 [» ]
ProteinModelPortali Q8K4J6.
SMRi Q8K4J6. Positions 14-126, 371-433.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 230180. 2 interactions.
IntActi Q8K4J6. 4 interactions.

PTM databases

PhosphoSitei Q8K4J6.

Proteomic databases

PaxDbi Q8K4J6.
PRIDEi Q8K4J6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000109579 ; ENSMUSP00000105207 ; ENSMUSG00000042292 . [Q8K4J6-1 ]
ENSMUST00000134469 ; ENSMUSP00000119530 ; ENSMUSG00000042292 . [Q8K4J6-2 ]
ENSMUST00000149582 ; ENSMUSP00000117745 ; ENSMUSG00000042292 . [Q8K4J6-2 ]
GeneIDi 223701.
KEGGi mmu:223701.
UCSCi uc007wwc.1. mouse. [Q8K4J6-1 ]

Organism-specific databases

CTDi 57591.
MGIi MGI:2384495. Mkl1.

Phylogenomic databases

eggNOGi NOG82832.
GeneTreei ENSGT00530000063195.
HOGENOMi HOG000038001.
HOVERGENi HBG036493.
InParanoidi Q642U1.
OMAi AQMDLEH.
OrthoDBi EOG7FR7G1.
PhylomeDBi Q8K4J6.
TreeFami TF326024.

Miscellaneous databases

ChiTaRSi MKL1. mouse.
EvolutionaryTracei Q8K4J6.
NextBioi 376834.
PROi Q8K4J6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8K4J6.
Bgeei Q8K4J6.
CleanExi MM_MKL1.
Genevestigatori Q8K4J6.

Family and domain databases

Gene3Di 1.10.720.30. 1 hit.
InterProi IPR004018. RPEL_repeat.
IPR003034. SAP_dom.
[Graphical view ]
Pfami PF02755. RPEL. 3 hits.
PF02037. SAP. 1 hit.
[Graphical view ]
SMARTi SM00707. RPEL. 3 hits.
SM00513. SAP. 1 hit.
[Graphical view ]
PROSITEi PS51073. RPEL. 3 hits.
PS50800. SAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiMKL1_MOUSE
AccessioniPrimary (citable) accession number: Q8K4J6
Secondary accession number(s): Q642U1
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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